7qsc

GTPase IN COMPLEX WITH GDP.MGF3-

Method: X-RAY DIFFRACTION Dmax: 94.2 Å Quality: GOOD

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

Rho GTPase-activating protein 1

Homo sapiens

UniProt Q07960

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 198–439 Chain C; UniProt 198–439 Mutation:R85A Transforming protein RhoA × 2 (P61586) GDP GUANOSINE-5'-DIPHOSPHATE × 2 MGF TRIFLUOROMAGNESATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Protein stock of RhoA-Y34F3Y 0.7 mM, RhoGAP-R85A 0.7 mM in a buffer of BisTris-HCl, pH 6.0, NaCl 150 mM, MgCl2 5 mM, NaF 10 mM, DTT 1 mM mixed 1:1.2 ratio with the precipitant solution of 0.1 M BisTris-HCl, pH 5.8, PEG3350 26% (w/v). Resolution 1.91 Å R-free 0.294

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.

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

View Construct and Data Evidence
UniProt name RHG01_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–244; UniProt 198–439 Author chain C; PDBConstruct 3–244; UniProt 198–439

Transforming protein RhoA

Homo sapiens

UniProt P61586

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–193 Chain D; UniProt 2–193 Mutation:Y34(F3Y) Non-standard monomer:Yes (specific site not provided by mmCIF) Rho GTPase-activating protein 1 × 2 (Q07960) GDP GUANOSINE-5'-DIPHOSPHATE × 2 MGF TRIFLUOROMAGNESATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Protein stock of RhoA-Y34F3Y 0.7 mM, RhoGAP-R85A 0.7 mM in a buffer of BisTris-HCl, pH 6.0, NaCl 150 mM, MgCl2 5 mM, NaF 10 mM, DTT 1 mM mixed 1:1.2 ratio with the precipitant solution of 0.1 M BisTris-HCl, pH 5.8, PEG3350 26% (w/v). Resolution 1.91 Å R-free 0.294

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.

129 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–192; UniProt 2–193 Author chain D; PDBConstruct 1–192; UniProt 2–193

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.

SAXS scattering curve SAXS Profile

SAXS profile for 7qsc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qsc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qsc
Deposition date deposition_date2022-01-13
Structure title titleGTPase IN COMPLEX WITH GDP.MGF3-
Keywords keywordsSmall G Protein, GTPase, Transition state analogue, metal fluoride complexes, fluoro-tyrosine, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.76
Radius of gyration Rg (electron density) rg_electron27.90
Forward intensity I(0) i0111338000.00
Molecular weight molecular_weight84076.0 kDa
Excluded volume excluded_volume105550 ų
Envelope volume envelope_volume127390 ų
Hydration-shell volume shell_volume37315 ų
Envelope diameter envelope_diameter99.4
Shell Rg shell_rg35.97
Envelope Rg envelope_rg27.82
Shape Rg shape_rg27.92
Total Rg total_rg28.60
Total atoms total_atoms5913
Residues n_residues729
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax94.2
Rg (real space) rg_real28.67
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real1.1130e+08
I(0) uncertainty (real space) i0_real_error1.4780e+06
Rg (reciprocal space) rg_reciprocal28.71
I(0) (reciprocal space) i0_reciprocal111300000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.250
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55630000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)