The domain within your query sequence starts at position 19 and ends at position 185; the E-value for the RAS domain shown below is 7.95e-114.
All catalytic sites are present in this domain. Check the literature (PubMed 1785141 12927549 ) for details.
SREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKIRIRIDDEPANLDILDTAG QAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYRVRRTDDTPVVLVGNKSDL KQLRQVSKEEGLSLAREFSCPFFETSAAYRYYIDDVFHALVREIRKK
RASRas subfamily of RAS small GTPases |
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| SMART accession number: | SM00173 |
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| Description: | Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades |
| Family alignment: |
There are 10915 RAS domains in 10905 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Taxonomic distribution of proteins containing RAS domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with RAS domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing RAS domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
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Binding / catalysis: GTP-hydrolysis
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Downward J
- Ras signalling and apoptosis.
- Curr Opin Genet Dev. 1998; 8: 49-54
- Display abstract
Activated Ras proteins have either positive or negative effects on the regulation of apoptosis depending on cell type and other factors. In part, this is due to the ability of Ras to control directly multiple effector pathways, including PI3-kinase, which provides a universal survival signal, and Raf, which can inhibit survival. The mechanisms remain partly unclear, however, especially with regard to Raf effects on apoptosis regulation. Recently Ras has been shown to be able to protect cells from apoptosis either through activation of PKB/Akt via PI3-kinase, or through activation of NF-kappa B.
- Lloyd AC
- Ras versus cyclin-dependent kinase inhibitors.
- Curr Opin Genet Dev. 1998; 8: 43-8
- Display abstract
In the past year, complex interactions between Ras and the cell cycle have been identified. In primary cells, activated Ras induces a cell-cycle arrest via the induction of cyclin-dependent kinase inhibitors (CDKIs). Oncogenic changes that cooperate with Ras act by neutralising CDKIs by various mechanisms. In the absence of a negative growth signal from Ras, such as in most immortalised cell lines, Ras acts positively on the cell cycle. Insights have been made into the mechanisms by which Ras abrogates remaining cell-cycle controls.
- Wittinghofer A, Pai EF
- The structure of Ras protein: a model for a universal molecular switch.
- Trends Biochem Sci. 1991; 16: 382-7
- Display abstract
X-ray crystallography has revealed the molecular architecture of the cellular and oncogenic forms of p21Ha-ras, the protein encoded by the human Ha-ras gene, in both its active (GTP-bound) and in its inactive (GDP-bound) forms. From comparison of these two structures, a mechanism is suggested for the GTPase hydrolysis reaction that triggers the conformational change necessary for signal transduction. The structures have also allowed identification of the structural consequences of point mutations and the way in which they interfere with the intrinsic GTPase activity of p21ras. The p21ras structure is similar to that of the G-domain of elongation factor Tu (EF-Tu) from Escherichia coli, suggesting that p21ras can serve as a good model for other guanine nucleotide binding proteins.
- Schlichting I et al.
- Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis.
- Nature. 1990; 345: 309-15
- Display abstract
Crystals of Ha-Ras p21 with caged GTP at the active site have been used to investigate the conformational changes of p21 on GTP hydrolysis. The structure of the short-lived p21.GTP complex was determined by Laue diffraction methods. After GTP hydrolysis, substantial structural changes occur in the parts of the molecule implicated in the interaction with GTPase-activating protein. The trigger for this process seems to be a change in coordination of the active-site Mg2+ ion as a result of loss of the gamma-phosphate of GTP.
- Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A
- Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation.
- Nature. 1989; 341: 209-14
- Display abstract
The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1-166) complexed to the guanosine triphosphate analogue guanosine-5'-(beta, gamma-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 A. The topological order of secondary structure elements is the same as that of the guanine-nucleotide-binding domain of bacterial elongation factor EF-Tu. Many interactions between nucleotide and protein have been identified. The effects of point mutations and the conservation of amino-acid sequence in the guanine-nucleotide-binding proteins are discussed.
- Shih TY, Papageorge AG, Stokes PE, Weeks MO, Scolnick EM
- Guanine nucleotide-binding and autophosphorylating activities associated with the p21src protein of Harvey murine sarcoma virus.
- Nature. 1980; 287: 686-91
- Display abstract
The purified p21src protein of Harvey sarcoma virus shows a guanine nucleotide-binding activity and, in addition, at elevated temperature an autophosphorylating activity at a threonine residue using as phosphoryl donor GTP or dGTP but not ATP or dATP. These biochemical activities are unique among those associated with transforming proteins of RNA-containing or DNA-containing tumour viruses.
- Disease (disease genes where sequence variants are found in this domain)
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SwissProt sequences and OMIM curated human diseases associated with missense mutations within the RAS domain.
Protein Disease Ras-related protein R-Ras2 (P62070) (SMART) OMIM:600098: ONCOGENE TC21 GTPase KRas (P01116) (SMART) OMIM:190070: Colorectal adenoma ; Colorectal cancer UNKNOWN (SMART) OMIM:190070: Colorectal adenoma ; Colorectal cancer GTPase HRas (P01112) (SMART) OMIM:190020: Bladder cancer
OMIM:109800:GTPase NRas (P01111) (SMART) OMIM:164790: Colorectal cancer Ras-related protein Rab-27A (P51159) (SMART) OMIM:603868: Griscelli syndrome
OMIM:214450: - Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 6.97 map04010 MAPK signaling pathway 5.61 map04530 Tight junction 5.61 map04810 Regulation of actin cytoskeleton 4.55 map04910 Insulin signaling pathway 4.24 map05211 Renal cell carcinoma 4.24 map04720 Long-term potentiation 2.88 map05219 Bladder cancer 2.88 map05216 Thyroid cancer 2.88 map04664 Fc epsilon RI signaling pathway 2.88 map05213 Endometrial cancer 2.88 map04370 VEGF signaling pathway 2.88 map04912 GnRH signaling pathway 2.88 map04662 B cell receptor signaling pathway 2.88 map05212 Pancreatic cancer 2.88 map05220 Chronic myeloid leukemia 2.88 map05215 Prostate cancer 2.88 map05214 Glioma 2.88 map04012 ErbB signaling pathway 2.88 map04660 T cell receptor signaling pathway 2.88 map04540 Gap junction 2.88 map05221 Acute myeloid leukemia 2.88 map04916 Melanogenesis 2.88 map04730 Long-term depression 2.88 map04360 Axon guidance 2.88 map05223 Non-small cell lung cancer 2.88 map05218 Melanoma 2.88 map04650 Natural killer cell mediated cytotoxicity 2.12 map04510 Focal adhesion 1.67 map04150 mTOR signaling pathway 1.36 map04670 Leukocyte transendothelial migration 1.06 map05210 Colorectal cancer 1.06 map04320 Dorso-ventral axis formation 1.06 map04914 Progesterone-mediated oocyte maturation This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with RAS domain which could be assigned to a KEGG orthologous group, and not all proteins containing RAS domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of RAS domains in PDB
PDB code Main view Title 121p 
STRUKTUR UND GUANOSINTRIPHOSPHAT-HYDROLYSEMECHANISMUS DES C-TERMINAL VERKUERZTEN MENSCHLICHEN KREBSPROTEINS P21-H-RAS 1aa9 
HUMAN C-HA-RAS(1-171)(DOT)GDP, NMR, MINIMIZED AVERAGE STRUCTURE 1agp 
THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLY-12 MUTANT OF P21-H-RAS 1bkd 
COMPLEX OF HUMAN H-RAS WITH HUMAN SOS-1 1c1y 
CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD). 1clu 
H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA,GAMMA-IMIDO-GTP 1crp 
THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY 1crq 
THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY 1crr 
THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY 1ctq 
STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K 1gnp 
X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP 1gnq 
X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP 1gnr 
X-RAY CRYSTAL STRUCTURE ANALYSIS OF THE CATALYTIC DOMAIN OF THE ONCOGENE PRODUCT P21H-RAS COMPLEXED WITH CAGED GTP AND MANT DGPPNHP 1gua 
HUMAN RAP1A, RESIDUES 1-167, DOUBLE MUTANT (E30D,K31E) COMPLEXED WITH GPPNHP AND THE RAS-BINDING-DOMAIN OF HUMAN C-RAF1, RESIDUES 51-131 1he8 
Ras G12V - PI 3-kinase gamma complex 1iaq 
C-H-RAS P21 PROTEIN MUTANT WITH THR 35 REPLACED BY SER (T35S) COMPLEXED WITH GUANOSINE-5'-[B,G-IMIDO] TRIPHOSPHATE 1ioz 
Crystal Structure of the C-HA-RAS Protein Prepared by the Cell-Free Synthesis 1jah 
H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,GAMMA-METHYLENE] TRIPHOSPHATE AND MAGNESIUM 1jai 
H-RAS P21 PROTEIN MUTANT G12P, COMPLEXED WITH GUANOSINE-5'-[BETA,GAMMA-METHYLENE] TRIPHOSPHATE AND MANGANESE 1k8r 
Crystal structure of Ras-Bry2RBD complex 1kao 
CRYSTAL STRUCTURE OF THE SMALL G PROTEIN RAP2A WITH GDP 1lf0 
Crystal Structure of RasA59G in the GTP-bound form 1lf5 
Crystal Structure of RasA59G in the GDP-bound Form 1lfd 
CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS 1nvu 
Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS 1nvv 
Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS 1nvw 
Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS 1nvx 
Structural evidence for feedback activation by RasGTP of the Ras-specific nucleotide exchange factor SOS 1p2s 
H-Ras 166 in 50% 2,2,2 triflouroethanol 1p2t 
H-Ras 166 in Aqueous mother liqour, RT 1p2u 
H-Ras in 50% isopropanol 1p2v 
H-RAS 166 in 60 % 1,6 hexanediol 1plj 
CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS 1plk 
CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS 1pll 
CRYSTALLOGRAPHIC STUDIES ON P21H-RAS USING SYNCHROTRON LAUE METHOD: IMPROVEMENT OF CRYSTAL QUALITY AND MONITORING OF THE GTPASE REACTION AT DIFFERENT TIME POINTS 1q21 
CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP 1qra 
STRUCTURE OF P21RAS IN COMPLEX WITH GTP AT 100 K 1rvd 
H-RAS COMPLEXED WITH DIAMINOBENZOPHENONE-BETA,GAMMA-IMIDO-GTP 1u8y 
CRystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap 1u8z 
Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap 1u90 
Crystal structures of Ral-GppNHp and Ral-GDP reveal two novel binding sites that are also present in Ras and Rap 1uad 
Crystal structure of the RalA-GppNHp-Sec5 Ral-binding domain complex 1wq1 
RAS-RASGAP COMPLEX 1x1r 
Crystal structure of M-Ras in complex with GDP 1x1s 
Crystal structure of M-Ras in complex with GppNHp 1xcm 
Crystal structure of the GppNHp-bound H-Ras G60A mutant 1xd2 
Crystal Structure of a ternary Ras:SOS:Ras*GDP complex 1xj0 
Crystal Structure of the GDP-bound form of the RasG60A mutant 1xtq 
Structure of small GTPase human Rheb in complex with GDP 1xtr 
Structure of small GTPase human Rheb in complex with GppNHp 1xts 
Structure of small GTPase human Rheb in complex with GTP 1zc3 
Crystal structure of the Ral-binding domain of Exo84 in complex with the active RalA 1zc4 
Crystal structure of the Ral-binding domain of Exo84 in complex with the active RalA 1zvq 
Structure of the Q61G mutant of Ras in the GDP-bound form 1zw6 
Crystal Structure of the GTP-bound form of RasQ61G 221p 
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES 2a78 
Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme 2a9k 
Crystal structure of the C3bot-NAD-RalA complex reveals a novel type of action of a bacterial exoenzyme 2atv 
The crystal structure of human RERG in the GDP bound state 2bov 
Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase 2c5l 
Structure of PLC epsilon Ras association domain with hRas 2ce2 
CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GDP 2cl0 
CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GppNHp 2cl6 
CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH S-caged GTP 2cl7 
CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GTP 2clc 
CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GTP (2) 2cld 
CRYSTAL STRUCTURE ANALYSIS OF A FLUORESCENT FORM OF H-RAS P21 IN COMPLEX WITH GDP (2) 2erx 
Crystal Structure of DiRas2 in Complex With GDP and Inorganic Phosphate 2ery 
The crystal structure of the Ras related protein RRas2 (RRAS2) in the GDP bound state 2evw 
Crystal structure analysis of a fluorescent form of H-Ras p21 in complex with R-caged GTP 2fn4 
The crystal structure of human Ras-related protein, RRAS, in the GDP-bound state 2gf0 
The crystal structure of the human DiRas1 GTPase in the inactive GDP bound state 2ke5 
Solution structure and dynamics of the small GTPase Ralb in its active conformation: significance for effector protein binding 2kwi 
RalB-RLIP76 (RalBP1) complex 2l0x 
Solution structure of the 21 kDa GTPase RHEB bound to GDP 2lcf 
Solution structure of GppNHp-bound H-RasT35S mutant protein 2lwi 
Solution structure of H-RasT35S mutant protein in complex with Kobe2601 2msc 
2MSC 2msd 
2MSD 2mse 
2MSE 2n42 
2N42 2n46 
2N46 2q21 
CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP 2quz 
Crystal Structure of the activating H-RasK117R mutant in Costello Syndrome, bound to Mg-GDP 2rap 
THE SMALL G PROTEIN RAP2A IN COMPLEX WITH GTP 2rga 
Crystal structure of H-RasQ61I-GppNHp 2rgb 
Crystal structure of H-RasQ61K-GppNHp 2rgc 
Crystal structure of H-RasQ61V-GppNHp 2rgd 
Crystal structure of H-RasQ61L-GppNHp 2rge 
Crystal structure of H-Ras-GppNHp 2rgg 
Crystal structure of H-RasQ61I-GppNHp, trigonal crystal form 2rhd 
Crystal structure of Cryptosporidium parvum small GTPase RAB1A 2uzi 
Crystal structure of HRAS(G12V) - anti-RAS Fv complex 2vh5 
CRYSTAL STRUCTURE OF HRAS(G12V) - ANTI-RAS FV (disulfide free mutant) COMPLEX 2x1v 
Crystal Structure of the activating H-Ras I163F mutant in Costello Syndrome, bound to MG-GDP 3brw 
Structure of the Rap-RapGAP complex 3cf6 
Structure of Epac2 in complex with cyclic-AMP and Rap 3con 
Crystal structure of the human NRAS GTPase bound with GDP 3ddc 
Crystal Structure of NORE1A in Complex with RAS 3gft 
Human K-Ras in complex with a GTP analogue 3i3s 
Crystal Structure of H-Ras with Thr50 replaced by Isoleucine 3k8y 
Allosteric modulation of H-Ras GTPase 3k9l 
Allosteric modulation of H-Ras GTPase 3k9n 
Allosteric modulation of H-Ras GTPase 3kkm 
Crystal structure of H-Ras T35S in complex with GppNHp 3kkn 
Crystal structure of H-Ras T35S in complex with GppNHp 3kko 
Crystal structure of M-Ras P40D/D41E/L51R in complex with GppNHp 3kkp 
Crystal structure of M-Ras P40D in complex with GppNHp 3kkq 
Crystal structure of M-Ras P40D in complex with GDP 3kuc 
Complex of Rap1A(E30D/K31E)GDP with RafRBD(A85K/N71R) 3kud 
Complex of Ras-GDP with RafRBD(A85K) 3l8y 
Complex of Ras with cyclen 3l8z 
H-Ras wildtype new crystal form 3lbh 
Ras soaked in Calcium Acetate 3lbi 
Ras soaked in Magnesium Acetate and back soaked in Calcium Acetate 3lbn 
Ras soaked in Magnesium Acetate 3lo5 
Crystal Structure of the dominant negative S17N mutant of Ras 3oes 
Crystal structure of the small GTPase RhebL1 3oiu 
H-RasQ61L with allosteric switch in the "on" state 3oiv 
H-RasG12V with allosteric switch in the "off" state 3oiw 
H-RasG12V with allosteric switch in the "on" state 3pir 
Crystal structure of M-RasD41E in complex with GppNHp (type 1) 3pit 
Crystal structure of M-RasD41E in complex with GppNHp (type 2) 3rap 
The small G protein Rap2 in a non catalytic complex with GTP 3rry 
H-Ras crosslinked control, soaked in aqueous solution: one of 10 in MSCS set 3rrz 
H-Ras in 70% glycerol: one of 10 in MSCS set 3rs0 
H-Ras soaked in neat cyclopentanol: one of 10 in MSCS set 3rs2 
H-Ras soaked in 50% 2,2,2-trifluoroethanol: one of 10 in MSCS set 3rs3 
H-Ras soaked in neat hexane: 1 of 10 in MSCS set 3rs4 
H-Ras soaked in 60% 1,6-hexanediol: 1 of 10 in MSCS set 3rs5 
H-Ras soaked in 55% dimethylformamide: 1 of 10 in MSCS set 3rs7 
H-Ras soaked in 50% isopropanol: 1 of 10 in MSCS set 3rsl 
H-Ras soaked in 90% R,S,R-bisfuranol: one of 10 in MSCS set 3rso 
H-Ras soaked in 20% S,R,S-bisfuranol: 1 of 10 in MSCS set 3sea 
Structure of Rheb-Y35A mutant in GDP- and GMPPNP-bound forms 3t5g 
Structure of fully modified farnesylated Rheb in complex with PDE6D 3tgp 
Room temperature H-ras 3v4f 
H-Ras PEG 400/CaCl2, ordered off 3x1w 
3X1W 3x1x 
3X1X 3x1y 
3X1Y 3x1z 
3X1Z 421p 
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES 4dlr 
H-Ras PEG 400/Ca(OAc)2, ordered off 4dls 
H-Ras Set 1 CaCl2 'Mixed' 4dlt 
H-Ras Set 2 Ca(OAc)2, on 4dlu 
H-Ras Set 1 Ca(OAc)2, on 4dlv 
H-Ras Set 2 CaCl2/DTT, ordered off 4dlw 
H-Ras Set 2 Ca(OAc)2/DTT, on 4dlx 
H-Ras Set 1 CaCl2/DTE, ordered off 4dly 
Set 1 CaCl2/DTT, ordered off 4dlz 
H-Ras Set 2 Ca(OAc)2/DTE, ordered off 4dsn 
Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity 4dso 
Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity 4dst 
Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity 4dsu 
Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-mediated nucleotide exchange activity 4dxa 
Co-crystal structure of Rap1 in complex with KRIT1 4efl 
Crystal structure of H-Ras WT in complex with GppNHp (state 1) 4efm 
Crystal structure of H-Ras G12V in complex with GppNHp (state 1) 4efn 
Crystal structure of H-Ras Q61L in complex with GppNHp (state 1) 4epr 
Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-Mediated Activation. 4ept 
Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation 4epv 
Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation 4epw 
Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation 4epx 
Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation 4epy 
Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation 4g0n 
Crystal Structure of wt H-Ras-GppNHp bound to the RBD of Raf Kinase 4g3x 
Crystal Structure of Q61L H-Ras-GppNHp bound to the RBD of Raf Kinase 4hdo 
Crystal structure of the binary Complex of KRIT1 bound to the Rap1 GTPase 4hdq 
Crystal Structure of the Ternary Complex of KRIT1 bound to both the Rap1 GTPase and the Heart of Glass (HEG1) cytoplasmic tail 4k81 
Crystal structure of the Grb14 RA and PH domains in complex with GTP-loaded H-Ras 4klz 
4KLZ 4ku4 
Crystal Structure of a Ras-like Protein from Cryphonectria parasitica in Complex with GDP 4kvg 
Crystal structure of RIAM RA-PH domains in complex with GTP bound Rap1 4l8g 
Crystal Structure of K-Ras G12C, GDP-bound 4l9s 
Crystal Structure of H-Ras G12C, GDP-bound 4l9w 
Crystal Structure of H-Ras G12C, GMPPNP-bound 4ldj 
4LDJ 4lpk 
Crystal Structure of K-Ras WT, GDP-bound 4lrw 
Crystal Structure of K-Ras G12C (cysteine-light), GDP-bound 4luc 
Crystal Structure of small molecule disulfide 6 bound to K-Ras G12C 4lv6 
Crystal Structure of small molecule disulfide 4 covalently bound to K-Ras G12C 4lyf 
Crystal Structure of small molecule vinylsulfonamide 8 covalently bound to K-Ras G12C 4lyh 
Crystal Structure of small molecule vinylsulfonamide 9 covalently bound to K-Ras G12C 4lyj 
Crystal Structure of small molecule vinylsulfonamide 9 covalently bound to K-Ras G12C, alternative space group 4m1o 
Crystal Structure of small molecule vinylsulfonamide 7 covalently bound to K-Ras G12C 4m1s 
Crystal Structure of small molecule vinylsulfonamide 13 covalently bound to K-Ras G12C 4m1t 
Crystal Structure of small molecule vinylsulfonamide 14 covalently bound to K-Ras G12C 4m1w 
Crystal Structure of small molecule vinylsulfonamide covalently bound to K-Ras G12C 4m1y 
Crystal Structure of small molecule vinylsulfonamide 15 covalently bound to K-Ras G12C 4m21 
Crystal Structure of small molecule acrylamide 11 covalently bound to K-Ras G12C 4m22 
Crystal Structure of small molecule acrylamide 16 covalently bound to K-Ras G12C 4m8n 
Crystal Structure of PlexinC1/Rap1B Complex 4mgi 
4MGI 4mgk 
4MGK 4mgy 
4MGY 4mgz 
4MGZ 4mh0 
4MH0 4nmm 
4NMM 4nyi 
Approach for Targeting Ras with Small Molecules that Activate SOS-Mediated Nucleotide Exchange 4nyj 
Approach for Targeting Ras with Small Molecules that Activate SOS-Mediated Nucleotide Exchange 4nym 
Approach for Targeting Ras with Small Molecules that Activate SOS-Mediated Nucleotide Exchange 4o25 
Structure of Wild Type Mus musculus Rheb bound to GTP 4o2l 
Structure of Mus musculus Rheb G63A mutant bound to GTP 4o2r 
Structure of Mus musculus Rheb G63V mutant bound to GDP 4obe 
4OBE 4pzy 
4PZY 4pzz 
4PZZ 4q01 
4Q01 4q02 
4Q02 4q03 
4Q03 4q21 
MOLECULAR SWITCH FOR SIGNAL TRANSDUCTION: STRUCTURAL DIFFERENCES BETWEEN ACTIVE AND INACTIVE FORMS OF PROTOONCOGENIC RAS PROTEINS 4ql3 
4QL3 4rsg 
4RSG 4tq9 
4TQ9 4tqa 
4TQA 4uru 
4URU 4urv 
4URV 4urw 
4URW 4urx 
4URX 4ury 
4URY 4urz 
4URZ 4us0 
4US0 4us1 
4US1 4us2 
4US2 4wa7 
4WA7 4xvq 
4XVQ 4xvr 
4XVR 521p 
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES 5b2z 
5B2Z 5b30 
5B30 5cm8 
5CM8 5cm9 
5CM9 5e95 
5E95 5f2e 
5F2E 5kho 
5KHO 5p21 
REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS 5tar 
5TAR 5tb5 
5TB5 621p 
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES 6q21 
MOLECULAR SWITCH FOR SIGNAL TRANSDUCTION: STRUCTURAL DIFFERENCES BETWEEN ACTIVE AND INACTIVE FORMS OF PROTOONCOGENIC RAS PROTEINS 721p 
THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES 821p 
THREE-DIMENSIONAL STRUCTURES AND PROPERTIES OF A TRANSFORMING AND A NONTRANSFORMING GLYCINE-12 MUTANT OF P21H-RAS - Links (links to other resources describing this domain)
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PFAM ras