6bc0

A Complex between PH Domain of p190RhoGEF and Activated RhoA Bound to a GTP Analog

Method: X-RAY DIFFRACTION Dmax: 81.1 Å Quality: GOOD

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

Rho guanine nucleotide exchange factor 28

Homo sapiens

UniProt Q8N1W1

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 1049–1194 Not recorded Transforming protein RhoA × 1 (P61586) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20-24% PEG 3350, 100mM TrisCl, 200mM NaCl Resolution 2.20 Å R-free 0.281

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARG28_HUMAN
Isoform Q8N1W1-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–150; UniProt 1049–1194

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 F; UniProt 1–181 Not recorded Rho guanine nucleotide exchange factor 28 × 1 (Q8N1W1) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20-24% PEG 3350, 100mM TrisCl, 200mM NaCl Resolution 2.20 Å R-free 0.281

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 F; PDBConstruct 5–185; UniProt 1–181

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 6bc0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bc0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6bc0
Deposition date deposition_date2017-10-20
Structure title titleA Complex between PH Domain of p190RhoGEF and Activated RhoA Bound to a GTP Analog
Keywords keywordsRho GTPase Guanine Nucleotide Exchange Factors RhoGEF Pleckstrin Homology PH domain, 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_guinier23.33
Radius of gyration Rg (electron density) rg_electron22.62
Forward intensity I(0) i022593100.00
Molecular weight molecular_weight36105.0 kDa
Excluded volume excluded_volume45227 ų
Envelope volume envelope_volume55543 ų
Hydration-shell volume shell_volume21359 ų
Envelope diameter envelope_diameter81.8
Shell Rg shell_rg28.82
Envelope Rg envelope_rg23.09
Shape Rg shape_rg22.61
Total Rg total_rg23.48
Total atoms total_atoms5068
Residues n_residues310
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 dmax81.1
Rg (real space) rg_real23.47
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.2590e+07
I(0) uncertainty (real space) i0_real_error3.5080e+05
Rg (reciprocal space) rg_reciprocal23.43
I(0) (reciprocal space) i0_reciprocal22590000.0000
Solution quality estimate total_estimate0.8393
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.533
Kurtosis Kurtosis kurtosis-0.163
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4609000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.698; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.919

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6bc0f_
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_id6bc0A00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id6bc0F00
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)