SAXSdb — 6way

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ras GTPase-activating protein 1

Homo sapiens

UniProt P20936

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 340–444	Mutation：C372S, C402S	Rho GTPase-activating protein 35 × 1 （Q9NRY4）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；1.2 M Sodium citrate tribasic dihydrate, 0.1 M Tris pH 8.5	Resolution 1.50 Å R-free 0.190

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 6WAY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WER RAS-GTPASE-ACTIVATING DOMAIN OF HUMAN P120GAP Deposited 1996-11-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 714–1047（334 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 714 - 1047	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；SEE REFERENCE 1, pH 6.5	Resolution 1.60 Å R-free 0.271
1WQ1 RAS-RASGAP COMPLEX Deposited 1997-07-03	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 714–1047（334 aa） Fragment：CATALYTIC DOMAIN, RESIDUES 714 - 1047	Not recorded	MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；SEE REF. DESCRIBING THE STRUCTURE, pH 8.	Resolution 2.50 Å R-free 0.319
2GQI Solution structure of the SH3 domain of human Ras GTPase-activating protein 1 Deposited 2006-04-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 282–339（58 aa） Fragment：SH3 domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.17mM 13C, 15N-labeled protein; 20mM d-Tris-HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3, 10% D2O; 90% H2O \| 10% D2O; 90% H2O	Resolution not provided
2GSB Solution structure of the second SH2 domain of human Ras GTPase-activating protein 1 Deposited 2006-04-26	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 341–446（106 aa） Fragment：SH2 domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；293 K；Ionic strength (raw mmCIF value) 120 mM；Pressure ambient NMR sample composition 1.27mM 13C, 15N-labeled protein; 20mM d-Tris-HCl (pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3, 10% D2O; 90% H2O \| 10% D2O; 90% H2O	Resolution not provided
2J05 Crystal structure of the RasGAP SH3 domain at 1.5 Angstrom resolution Deposited 2006-08-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 281–341（61 aa） Fragment：SH3 DOMAIN, RESIDUES 281-341 Chain B 281–341（61 aa） Fragment：SH3 DOMAIN, RESIDUES 281-341	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；100 MM KNO3, 100 MM TAPS, PH 9 AND 40% PEG 8000	Resolution 1.50 Å R-free 0.199
2J06 Crystal structure of the RasGAP SH3 domain at 1.8 Angstrom resolution Deposited 2006-08-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 281–341（61 aa） Fragment：SH3 DOMAIN, RESIDUES 281-341 Chain B 281–341（61 aa） Fragment：SH3 DOMAIN, RESIDUES 281-341	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；90 MM KNO3, 15.5% GLYCEROL, 90 MM TAPS, PH 9 AND 45.5% PEG8000	Resolution 1.80 Å R-free 0.240
2M51 NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1 Deposited 2013-02-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 281–341（61 aa） Fragment：UNP residues 281-341	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 0.798；Pressure ambient NMR sample composition 1.2 mM [U-98% 13C; U-98% 15N] protein, 20 mM sodium phosphate, 50 mM sodium chloride, 5 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4FSS Crystal structure of a RAS p21 protein activator (RASA1) from Homo sapiens at 2.25 A resolution Deposited 2012-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 281–341（61 aa） Fragment：SH3 domain residues 281-341	Non-standard monomer：Yes (specific site not provided by mmCIF)	PO4 PHOSPHATE ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；20.00% Glycerol, 1.600M NH4H2PO4, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.25 Å R-free 0.237
4FSS Crystal structure of a RAS p21 protein activator (RASA1) from Homo sapiens at 2.25 A resolution Deposited 2012-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 281–341（61 aa） Fragment：SH3 domain residues 281-341	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；20.00% Glycerol, 1.600M NH4H2PO4, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.25 Å R-free 0.237
4FSS Crystal structure of a RAS p21 protein activator (RASA1) from Homo sapiens at 2.25 A resolution Deposited 2012-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 281–341（61 aa） Fragment：SH3 domain residues 281-341	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；20.00% Glycerol, 1.600M NH4H2PO4, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 2.25 Å R-free 0.237
6PXB N-Terminal SH2 domain of the p120RasGAP Deposited 2019-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain F 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；21% PEG 10,000 0.1M Tris pH 8.0 0.2M Ammonium Acetate	Resolution 1.75 Å R-free 0.263
6PXB N-Terminal SH2 domain of the p120RasGAP Deposited 2019-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；21% PEG 10,000 0.1M Tris pH 8.0 0.2M Ammonium Acetate	Resolution 1.75 Å R-free 0.263
6PXB N-Terminal SH2 domain of the p120RasGAP Deposited 2019-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；21% PEG 10,000 0.1M Tris pH 8.0 0.2M Ammonium Acetate	Resolution 1.75 Å R-free 0.263
6PXB N-Terminal SH2 domain of the p120RasGAP Deposited 2019-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；21% PEG 10,000 0.1M Tris pH 8.0 0.2M Ammonium Acetate	Resolution 1.75 Å R-free 0.263
6PXB N-Terminal SH2 domain of the p120RasGAP Deposited 2019-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；21% PEG 10,000 0.1M Tris pH 8.0 0.2M Ammonium Acetate	Resolution 1.75 Å R-free 0.263
6PXB N-Terminal SH2 domain of the p120RasGAP Deposited 2019-07-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；21% PEG 10,000 0.1M Tris pH 8.0 0.2M Ammonium Acetate	Resolution 1.75 Å R-free 0.263
6PXC N-Terminal SH2 domain of the p120RasGAP bound to a p190RhoGAP phosphotyrosine peptide Deposited 2019-07-25	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 174–280（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；1.8M Sodium Malonate 0.1M Bis Tris 6.5 2% PEG MME 550	Resolution 1.60 Å R-free 0.210
6WAX C-terminal SH2 domain of p120RasGAP Deposited 2020-03-26	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 340–444（105 aa）	Mutation：C372S, C402S	SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；2.3 M Ammonium Sulfate, 0.1 M Bis Tris pH 6.5	Resolution 1.50 Å R-free 0.197
6WAX C-terminal SH2 domain of p120RasGAP Deposited 2020-03-26	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 340–444（105 aa）	Mutation：C372S, C402S	SO4 SULFATE ION × 1 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；2.3 M Ammonium Sulfate, 0.1 M Bis Tris pH 6.5	Resolution 1.50 Å R-free 0.197
8BOS Transition state analogue complex of small G protein and its GAP effector Deposited 2022-11-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 713–1042（330 aa）	Not recorded	GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 MG MAGNESIUM ION × 1 GAI GUANIDINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；precipitant: HEPES-Na 100 mM pH = 8.0, PEG3350 22% (w/v), (NH4)2SO4 20 mM, Gd-HCl 100 mM, NaF 20 mM protein buffer: HRas 0.400 mM, RasGAP 0.400 mM, HEPES-Na 20 mM, NaF 20 mM drop size: 5 uL, protein:precipitant ratio: 1:1.2	Resolution 2.10 Å R-free 0.280
8DGQ Crystal structure of p120RasGAP SH2-SH3-SH2 in complex with p190RhoGAP doubly phosphorylated peptide Deposited 2022-06-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 174–444（271 aa）	Not recorded	MLI MALONATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.5 M Sodium Malonate pH 5.0, 0.1 M sodium acetate trihydrate salt, 6% PEG 20,000	Resolution 1.95 Å R-free 0.256
8DGQ Crystal structure of p120RasGAP SH2-SH3-SH2 in complex with p190RhoGAP doubly phosphorylated peptide Deposited 2022-06-24	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 174–444（271 aa）	Not recorded	MLI MALONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.5 M Sodium Malonate pH 5.0, 0.1 M sodium acetate trihydrate salt, 6% PEG 20,000	Resolution 1.95 Å R-free 0.256
9BZ4 Crystal structure of the C2 and GAP domains of human p120RasGAP Deposited 2024-05-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 581–1047（467 aa） Fragment：UNP Residues 581-1047	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；0.2M Ammonium Phosphate Dibasic 0.1M MOPS pH 7.4 26% w/v PEG 3350	Resolution 2.45 Å R-free 0.284
9BZ4 Crystal structure of the C2 and GAP domains of human p120RasGAP Deposited 2024-05-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 581–1047（467 aa） Fragment：UNP Residues 581-1047	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；0.2M Ammonium Phosphate Dibasic 0.1M MOPS pH 7.4 26% w/v PEG 3350	Resolution 2.45 Å R-free 0.284
9BZ4 Crystal structure of the C2 and GAP domains of human p120RasGAP Deposited 2024-05-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 581–1047（467 aa） Fragment：UNP Residues 581-1047	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；0.2M Ammonium Phosphate Dibasic 0.1M MOPS pH 7.4 26% w/v PEG 3350	Resolution 2.45 Å R-free 0.284
9BZ4 Crystal structure of the C2 and GAP domains of human p120RasGAP Deposited 2024-05-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 581–1047（467 aa） Fragment：UNP Residues 581-1047	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；298 K；0.2M Ammonium Phosphate Dibasic 0.1M MOPS pH 7.4 26% w/v PEG 3350	Resolution 2.45 Å R-free 0.284

14 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RASA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–107； UniProt 340–444

Rho GTPase-activating protein 35

OrganismNot specified

UniProt Q9NRY4

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain V； UniProt 1086–1093	Non-standard monomer：Yes (specific site not provided by mmCIF)	Ras GTPase-activating protein 1 × 1 （P20936）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；1.2 M Sodium citrate tribasic dihydrate, 0.1 M Tris pH 8.5	Resolution 1.50 Å R-free 0.190

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 6WAY	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2K85 p190-A RhoGAP FF1 domain Deposited 2008-09-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 267–331（65 aa） Fragment：UNP residues 267-331	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；285 K；Ionic strength (raw mmCIF value) 0.2；Pressure ambient NMR sample composition 1 mM p190-A RhoGAP FF1 domain, 50 mM sodium phosphate, 150 mM sodium chloride, 0.5 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p190-A RhoGAP FF1 domain, 50 mM sodium phosphate, 150 mM sodium chloride, 0.5 mM sodium azide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p190-A RhoGAP FF1 domain, 50 mM sodium phosphate, 150 mM sodium chloride, 0.5 mM sodium azide, 100% D2O \| 100% D2O	Resolution not provided
3C5H Crystal structure of the Ras homolog domain of human GRLF1 (p190RhoGAP) Deposited 2008-01-31	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 13–249（237 aa） Fragment：Ras homolog domain: Residues 13-249	Not recorded	MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 UNX UNKNOWN LIGAND × 5	X-RAY DIFFRACTION X-ray crystallization conditions Native crystal, used for model refinement: 26% PEG 4000, 0.1M Tris-HCl, 0.2M Magnesium chloride, 0.1mM DTT, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K X-ray crystallization conditions Seleno-methionine derivative crystal, used for MAD phasing: 33% PEG 4000, 0.1M Tris-HCl, 0.2M Magnesium chloride, 0.1mM DTT, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K. A ten-fold excess of GppNHp was added to the protein samples prior to crystallization.	Resolution 1.80 Å R-free 0.247
3FK2 Crystal structure of the RhoGAP domain of human glucocorticoid receptor DNA-binding factor 1 Deposited 2008-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1212–1439（228 aa） Fragment：UNP residues 1212-1439	Not recorded	UNX UNKNOWN LIGAND × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；26% PEG 3350, 0.1M Bis-Tris, 0.2M lithium sulfate, 0.001M DTT, 1:100 (w/w) trypsin, pH 6.0, vapor diffusion, sitting drop, temperature 291K	Resolution 2.80 Å R-free 0.273
3FK2 Crystal structure of the RhoGAP domain of human glucocorticoid receptor DNA-binding factor 1 Deposited 2008-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1212–1439（228 aa） Fragment：UNP residues 1212-1439	Not recorded	UNX UNKNOWN LIGAND × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；26% PEG 3350, 0.1M Bis-Tris, 0.2M lithium sulfate, 0.001M DTT, 1:100 (w/w) trypsin, pH 6.0, vapor diffusion, sitting drop, temperature 291K	Resolution 2.80 Å R-free 0.273
3FK2 Crystal structure of the RhoGAP domain of human glucocorticoid receptor DNA-binding factor 1 Deposited 2008-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1212–1439（228 aa） Fragment：UNP residues 1212-1439	Not recorded	UNX UNKNOWN LIGAND × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；26% PEG 3350, 0.1M Bis-Tris, 0.2M lithium sulfate, 0.001M DTT, 1:100 (w/w) trypsin, pH 6.0, vapor diffusion, sitting drop, temperature 291K	Resolution 2.80 Å R-free 0.273
3FK2 Crystal structure of the RhoGAP domain of human glucocorticoid receptor DNA-binding factor 1 Deposited 2008-12-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 1212–1439（228 aa） Fragment：UNP residues 1212-1439	Not recorded	UNX UNKNOWN LIGAND × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；291 K；26% PEG 3350, 0.1M Bis-Tris, 0.2M lithium sulfate, 0.001M DTT, 1:100 (w/w) trypsin, pH 6.0, vapor diffusion, sitting drop, temperature 291K	Resolution 2.80 Å R-free 0.273
8DGQ Crystal structure of p120RasGAP SH2-SH3-SH2 in complex with p190RhoGAP doubly phosphorylated peptide Deposited 2022-06-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain U 1083–1111（29 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MLI MALONATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.5 M Sodium Malonate pH 5.0, 0.1 M sodium acetate trihydrate salt, 6% PEG 20,000	Resolution 1.95 Å R-free 0.256
8DGQ Crystal structure of p120RasGAP SH2-SH3-SH2 in complex with p190RhoGAP doubly phosphorylated peptide Deposited 2022-06-24	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain V 1083–1111（29 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	MLI MALONATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.5 M Sodium Malonate pH 5.0, 0.1 M sodium acetate trihydrate salt, 6% PEG 20,000	Resolution 1.95 Å R-free 0.256

4 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RHG35_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain V； PDBConstruct 2–9； UniProt 1086–1093

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6way
Deposition date deposition_date	2020-03-26
Structure title title	C-terminal SH2 domain of p120RasGAP in complex with p190RhoGAP phosphotyrosine peptide
Keywords keywords	SH2 domain, RasGAP, phosphopeptide, phosphotyrosine, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	15.25 Å
Radius of gyration Rg (electron density) rg_electron	13.63 Å
Forward intensity I(0) i0	3912110.00
Molecular weight molecular_weight	13426.0 kDa
Excluded volume excluded_volume	16583 Å³
Envelope volume envelope_volume	19000 Å³
Hydration-shell volume shell_volume	11867 Å³
Envelope diameter envelope_diameter	50.1 Å
Shell Rg shell_rg	19.42 Å
Envelope Rg envelope_rg	14.08 Å
Shape Rg shape_rg	13.59 Å
Total Rg total_rg	14.98 Å
Total atoms total_atoms	945
Residues n_residues	113
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	51.3 Å
Rg (real space) rg_real	15.15 Å
Rg uncertainty (real space) rg_real_error	0.28 Å
I(0) (real space) i0_real	3.9120e+06
I(0) uncertainty (real space) i0_real_error	4.7320e+04
Rg (reciprocal space) rg_reciprocal	15.15 Å
I(0) (reciprocal space) i0_reciprocal	3912000.0000
Solution quality estimate total_estimate	0.8610
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.8 Å
Skewness Skewness skewness	0.169
Kurtosis Kurtosis kurtosis	-0.205
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	776600.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.735; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.983

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Ras GTPase-activating protein 1
Molecular weight formula_weight	12467.9 kDa
Mutation mutation	C372S, C402S
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1188

GSGREEDPHEGKIWFHGKISKQEAYNLLMTVGQVSSFLVRPSDNTPGDYSLYFRTNENIQRFKISPTPNNQFMMGGRYYNSIGDIIDHYRKEQIVEGYYLKEPVPMQ

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	Human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Rho GTPase-activating protein 35
Molecular weight formula_weight	1015.0 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V

XDYAEPMDAX

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	197

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	6wayA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	505 — SHC Adaptor Protein
Homologous superfamily homologous superfamily	10 — SH2 domain

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8. Citations (1)

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Unit-cell length a length_a	63.119 Å
Unit-cell length b length_b	83.910 Å
Unit-cell length c length_c	54.239 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	27.278 Å
R factor r_factor	0.1658
R_work r_work	0.1645
R_free r_free	0.1903

fit	/app/data/saxs_computation/wa/6way/6way.fit
pddf	/app/data/pr_computation/wa/6way/6way.pr.out
profile	/app/data/saxs_computation/wa/6way/6way.dat

C-terminal SH2 domain of p120RasGAP in complex with p190RhoGAP phosphotyrosine peptide

1. Protein Identity and Related Structures Protein Identity & Related Structures

Ras GTPase-activating protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Rho GTPase-activating protein 35

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)