8bnt

The DH domain of ARHGEF2 bound to RhoA

Method: X-RAY DIFFRACTION Dmax: 74.7 Å Quality: EXCELLENT

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 1–184 Not recorded Rho guanine nucleotide exchange factor 2 × 1 (Q92974) DMS DIMETHYL SULFOXIDE × 5 FMT FORMIC ACID × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;2.6 M sodium formate, 100 mM Tris Resolution 1.40 Å R-free 0.175

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 2–185; UniProt 1–184

Rho guanine nucleotide exchange factor 2

Homo sapiens

UniProt Q92974

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 206–448 Not recorded Transforming protein RhoA × 1 (P61586) DMS DIMETHYL SULFOXIDE × 5 FMT FORMIC ACID × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;2.6 M sodium formate, 100 mM Tris Resolution 1.40 Å R-free 0.175

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.

59 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARHG2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–245; UniProt 206–448

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 8bnt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bnt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bnt
Deposition date deposition_date2022-11-25
Structure title titleThe DH domain of ARHGEF2 bound to RhoA
Keywords keywordsGTP, GDP, Guanine, cytoskeleton, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.10
Radius of gyration Rg (electron density) rg_electron22.73
Forward intensity I(0) i042711900.00
Molecular weight molecular_weight49898.0 kDa
Excluded volume excluded_volume62348 ų
Envelope volume envelope_volume76648 ų
Hydration-shell volume shell_volume27616 ų
Envelope diameter envelope_diameter77.6
Shell Rg shell_rg30.23
Envelope Rg envelope_rg23.00
Shape Rg shape_rg22.70
Total Rg total_rg23.72
Total atoms total_atoms3492
Residues n_residues424
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 dmax74.7
Rg (real space) rg_real23.94
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.2710e+07
I(0) uncertainty (real space) i0_real_error4.8950e+05
Rg (reciprocal space) rg_reciprocal23.98
I(0) (reciprocal space) i0_reciprocal42710000.0000
Solution quality estimate total_estimate0.9041
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8295000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)