3msx

Crystal structure of RhoA.GDP.MgF3 in complex with GAP domain of ArhGAP20

Method: X-RAY DIFFRACTION Dmax: 74.8 Å Quality: GOOD

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

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 A; UniProt 1–180 Mutation:F25N Rho GTPase-activating protein 20 × 1 (Q9P2F6) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MGF TRIFLUOROMAGNESATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Crystallization drop was 1:1 mixture of protein dissolved in 20 mM Tris, pH 8.5, 100 mM NaCl, 5 mM NaF, 5 mM MgCl2, 5mM 2-mercaptoethanol and 20 w/v% PEG 8000, 0.2 M NaCl, 0.17 M NH4Cl, 0.1 M phosphate citrate buffer. The crystallization reservoir was 20 w/v% PEG 8000, 0.2 M NaCl, 0.17 M NH4Cl, 0.1 M phosphate citrate buffer, vapor diffusion, sitting drop, temperature 293K Resolution 1.65 Å R-free 0.219

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–180; UniProt 1–180

Rho GTPase-activating protein 20

Homo sapiens

UniProt Q9P2F6

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 351–551 Fragment:GAP domain Transforming protein RhoA × 1 (P61586) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 MGF TRIFLUOROMAGNESATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Crystallization drop was 1:1 mixture of protein dissolved in 20 mM Tris, pH 8.5, 100 mM NaCl, 5 mM NaF, 5 mM MgCl2, 5mM 2-mercaptoethanol and 20 w/v% PEG 8000, 0.2 M NaCl, 0.17 M NH4Cl, 0.1 M phosphate citrate buffer. The crystallization reservoir was 20 w/v% PEG 8000, 0.2 M NaCl, 0.17 M NH4Cl, 0.1 M phosphate citrate buffer, vapor diffusion, sitting drop, temperature 293K Resolution 1.65 Å R-free 0.219

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name RHG20_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–201; UniProt 351–551

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 3msx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3msx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3msx
Deposition date deposition_date2010-04-29
Structure title titleCrystal structure of RhoA.GDP.MgF3 in complex with GAP domain of ArhGAP20
Keywords keywordsprotein-proten complex, transition state, GTPase, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.40
Radius of gyration Rg (electron density) rg_electron21.30
Forward intensity I(0) i030449100.00
Molecular weight molecular_weight42244.0 kDa
Excluded volume excluded_volume52880 ų
Envelope volume envelope_volume61643 ų
Hydration-shell volume shell_volume23959 ų
Envelope diameter envelope_diameter76.6
Shell Rg shell_rg28.26
Envelope Rg envelope_rg21.56
Shape Rg shape_rg21.31
Total Rg total_rg22.14
Total atoms total_atoms2962
Residues n_residues369
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 dmax74.8
Rg (real space) rg_real22.35
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real3.0450e+07
I(0) uncertainty (real space) i0_real_error3.8580e+05
Rg (reciprocal space) rg_reciprocal22.36
I(0) (reciprocal space) i0_reciprocal30450000.0000
Solution quality estimate total_estimate0.8775
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.346
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6996000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.815; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.958

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3msxa_
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
Domain ID domain_idd3msxb_
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.116.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3msxA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3msxB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology555 — Phosphatidylinositol 3-kinase; Chain A
Homologous superfamily homologous superfamily10 — Rho GTPase activation protein

8. Citations (1)

9. Files and Curves (10)