7g8c

ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1037511924

Method: X-RAY DIFFRACTION Dmax: 74.5 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) YXO 1-(difluoromethyl)-1H-indol-5-amine × 1 DMS DIMETHYL SULFOXIDE × 5 FMT FORMIC ACID × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;100 mM Tris, 2.6M sodium formate Resolution 2.18 Å R-free 0.255

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 Mutation:None Transforming protein RhoA × 1 (P61586) YXO 1-(difluoromethyl)-1H-indol-5-amine × 1 DMS DIMETHYL SULFOXIDE × 5 FMT FORMIC ACID × 10 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;100 mM Tris, 2.6M sodium formate Resolution 2.18 Å R-free 0.255

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 7g8c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7g8c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7g8c
Deposition date deposition_date2023-06-22
Structure title titleARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1037511924
Keywords keywordsSGC - Diamond I04-1 fragment screening, PanDDA, XChemExplorer, 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_guinier23.71
Radius of gyration Rg (electron density) rg_electron22.36
Forward intensity I(0) i040276900.00
Molecular weight molecular_weight48631.0 kDa
Excluded volume excluded_volume60855 ų
Envelope volume envelope_volume73891 ų
Hydration-shell volume shell_volume27062 ų
Envelope diameter envelope_diameter77.4
Shell Rg shell_rg29.75
Envelope Rg envelope_rg22.51
Shape Rg shape_rg22.33
Total Rg total_rg23.37
Total atoms total_atoms3404
Residues n_residues414
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 dmax74.5
Rg (real space) rg_real23.56
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real4.0280e+07
I(0) uncertainty (real space) i0_real_error5.2380e+05
Rg (reciprocal space) rg_reciprocal23.59
I(0) (reciprocal space) i0_reciprocal40280000.0000
Solution quality estimate total_estimate0.9027
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.1
Skewness Skewness skewness0.120
Kurtosis Kurtosis kurtosis-0.524
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9222000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7g8cA01
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)