5m6x

Crystal Structure of human RhoGAP mutated in its arginine finger (R85A) in complex with RhoA.GDP.MgF3- human

Method: X-RAY DIFFRACTION Dmax: 92.9 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 198–437 Not recorded Transforming protein RhoA × 1 (P61586) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;293 K;100 mM Bis Tris pH 5.5-6.5 20-25% (w/v) PEG3350 Resolution 2.40 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 198–437 Not recorded Transforming protein RhoA × 1 (P61586) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;293 K;100 mM Bis Tris pH 5.5-6.5 20-25% (w/v) PEG3350 Resolution 2.40 Å R-free 0.272

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 13 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 1–240; UniProt 198–437 Author chain H; PDBConstruct 1–240; UniProt 198–437

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 2–193 Not recorded Rho GTPase-activating protein 1 × 1 (Q07960) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;293 K;100 mM Bis Tris pH 5.5-6.5 20-25% (w/v) PEG3350 Resolution 2.40 Å R-free 0.272
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 2–193 Not recorded Rho GTPase-activating protein 1 × 1 (Q07960) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;293 K;100 mM Bis Tris pH 5.5-6.5 20-25% (w/v) PEG3350 Resolution 2.40 Å R-free 0.272

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 164 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 I; 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 5m6x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5m6x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5m6x
Deposition date deposition_date2016-10-26
Structure title titleCrystal Structure of human RhoGAP mutated in its arginine finger (R85A) in complex with RhoA.GDP.MgF3- human
Keywords keywordsRHOGAP, Arginine finger, RHOA, transition state, Signaling protein; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.79
Radius of gyration Rg (electron density) rg_electron27.93
Forward intensity I(0) i0110506000.00
Molecular weight molecular_weight83923.0 kDa
Excluded volume excluded_volume105460 ų
Envelope volume envelope_volume128660 ų
Hydration-shell volume shell_volume37611 ų
Envelope diameter envelope_diameter98.2
Shell Rg shell_rg36.03
Envelope Rg envelope_rg27.83
Shape Rg shape_rg27.95
Total Rg total_rg28.64
Total atoms total_atoms5904
Residues n_residues731
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 dmax92.9
Rg (real space) rg_real28.71
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.1050e+08
I(0) uncertainty (real space) i0_real_error1.7370e+06
Rg (reciprocal space) rg_reciprocal28.75
I(0) (reciprocal space) i0_reciprocal110500000.0000
Solution quality estimate total_estimate0.8962
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.419
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61460000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5m6xa_
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_idd5m6xb_
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.37.1.0 — automated matches
Domain ID domain_idd5m6xh_
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_idd5m6xi_
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.37.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id5m6xA00
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_id5m6xB00
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_id5m6xH00
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_id5m6xI00
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)