6r3v

Crystal Structure of RhoA-GDP-Pi in Complex with RhoGAP

Method: X-RAY DIFFRACTION Dmax: 74.4 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–439 Fragment:GTPASE ACTIVITING DOMAIN Transforming protein RhoA × 1 (P61586) PO4 PHOSPHATE ION × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;Equal amounts of reservoir solution containing 18% PEG2000 MME, 100 mM MES, pH 6.0, 10 mM MgCl2, 3 mM DTT, 3 mM NaN3, 120 mM ammonium sulphate and stock solution of the RhoA/RhoGAP protein complex at 800 mM in 20 mM Tris.HCl, pH 7.4, with 2 mM AlCl3, 10 mM MgCl2, and 20 mM NaF. Resolution 1.75 Å R-free 0.207

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 1–439; UniProt 1–439

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–193 Mutation:YES [F25N] Rho GTPase-activating protein 1 × 1 (Q07960) PO4 PHOSPHATE ION × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;Equal amounts of reservoir solution containing 18% PEG2000 MME, 100 mM MES, pH 6.0, 10 mM MgCl2, 3 mM DTT, 3 mM NaN3, 120 mM ammonium sulphate and stock solution of the RhoA/RhoGAP protein complex at 800 mM in 20 mM Tris.HCl, pH 7.4, with 2 mM AlCl3, 10 mM MgCl2, and 20 mM NaF. Resolution 1.75 Å R-free 0.207

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 1–193; UniProt 1–193

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 6r3v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6r3v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6r3v
Deposition date deposition_date2019-03-21
Structure title titleCrystal Structure of RhoA-GDP-Pi in Complex with RhoGAP
Keywords keywordsSMALL G PROTEIN, GTPASE, GTP HYDROLYSIS, PRODUCT COMPLEX, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.51
Radius of gyration Rg (electron density) rg_electron21.55
Forward intensity I(0) i030348700.00
Molecular weight molecular_weight42520.0 kDa
Excluded volume excluded_volume53288 ų
Envelope volume envelope_volume62184 ų
Hydration-shell volume shell_volume24008 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg28.46
Envelope Rg envelope_rg21.79
Shape Rg shape_rg21.55
Total Rg total_rg22.39
Total atoms total_atoms2986
Residues n_residues370
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 dmax74.4
Rg (real space) rg_real22.46
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real3.0350e+07
I(0) uncertainty (real space) i0_real_error3.9280e+05
Rg (reciprocal space) rg_reciprocal22.47
I(0) (reciprocal space) i0_reciprocal30350000.0000
Solution quality estimate total_estimate0.8873
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha7117000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6r3va_
Class classa — All alpha proteins
Fold Fold folda.116 — GTPase activation domain, GAP
Superfamily Superfamily superfamilya.116.1 — GTPase activation domain, GAP
Family Family familya.116.1.1 — BCR-homology GTPase activation domain (BH-domain)
Domain ID domain_idd6r3vb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (2 domains)

Domain ID domain_id6r3vA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology555 — Phosphatidylinositol 3-kinase; Chain A
Homologous superfamily homologous superfamily10 — Rho GTPase activation protein
Domain ID domain_id6r3vB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)