8i5f

Crystal structure of the DHR-2 domain of DOCK10 in complex with Cdc42 (T17N mutant)

Method: X-RAY DIFFRACTION Dmax: 159.9 Å Quality: GOOD

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

Dedicator of cytokinesis protein 10

Mus musculus

UniProt Q8BZN6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1664–2150 Chain B; UniProt 1664–2150 Not recorded Cell division control protein 42 homolog × 2 (P60953) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;PEG 8000, sodium chloride Resolution 2.80 Å R-free 0.296

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.

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

View Construct and Data Evidence
UniProt name DOC10_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–494; UniProt 1664–2150 Author chain B; PDBConstruct 8–494; UniProt 1664–2150

Cell division control protein 42 homolog

Homo sapiens

UniProt P60953

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–188 Chain D; UniProt 1–188 Mutation:T17N, C188S Dedicator of cytokinesis protein 10 × 2 (Q8BZN6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;PEG 8000, sodium chloride Resolution 2.80 Å R-free 0.296

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.

45 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC42_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 8–195; UniProt 1–188 Author chain D; PDBConstruct 8–195; UniProt 1–188

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 8i5f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i5f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i5f
Deposition date deposition_date2023-01-25
Structure title titleCrystal structure of the DHR-2 domain of DOCK10 in complex with Cdc42 (T17N mutant)
Keywords keywordsGEF, GTPase, Rho, Cdc42, Rac, 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_guinier45.50
Radius of gyration Rg (electron density) rg_electron45.60
Forward intensity I(0) i0275583000.00
Molecular weight molecular_weight140460.0 kDa
Excluded volume excluded_volume177380 ų
Envelope volume envelope_volume245350 ų
Hydration-shell volume shell_volume46995 ų
Envelope diameter envelope_diameter161.3
Shell Rg shell_rg46.58
Envelope Rg envelope_rg45.12
Shape Rg shape_rg45.58
Total Rg total_rg45.71
Total atoms total_atoms9889
Residues n_residues1221
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 dmax159.9
Rg (real space) rg_real45.90
Rg uncertainty (real space) rg_real_error2.12
I(0) (real space) i0_real2.7560e+08
I(0) uncertainty (real space) i0_real_error5.7310e+06
Rg (reciprocal space) rg_reciprocal45.50
I(0) (reciprocal space) i0_reciprocal275400000.0000
Solution quality estimate total_estimate0.7939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.780
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28180000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.599; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.532; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8i5fC01
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_id8i5fD01
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)