2wmo

Structure of the complex between DOCK9 and Cdc42.

Method: X-RAY DIFFRACTION Dmax: 91.8 Å Quality: GOOD

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

DEDICATOR OF CYTOKINESIS PROTEIN 9

HOMO SAPIENS

UniProt Q9BZ29

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 1605–1652 Chain A; UniProt 1676–2053 Fragment:DHR2 DOMAIN, RESIDUES 1605-1652,1676-2053 CELL DIVISION CONTROL PROTEIN 42 HOMOLOG × 2 (P60953) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.20 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DOCK9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–48; UniProt 1605–1652 Author chain A; PDBConstruct 49–426; UniProt 1676–2053

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 B; UniProt 1–188 Not recorded DEDICATOR OF CYTOKINESIS PROTEIN 9 × 2 (Q9BZ29) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.20 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.

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 B; PDBConstruct 3–190; 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 2wmo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wmo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2wmo
Deposition date deposition_date2009-07-02
Structure title titleStructure of the complex between DOCK9 and Cdc42.
Keywords keywords;POLYMORPHISM, CELL MEMBRANE, PHOSPHOPROTEIN, NUCLEOTIDE-BINDING, ALTERNATIVE SPLICING, GUANINE-NUCLEOTIDE RELEASING FACTOR, CELL CYCLE, METHYLATION, LIPOPROTEIN, COILED COIL, GTP-BINDING, GEFS, DOCK9, CDC42, MEMBRANE, PRENYLATION ;; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.80
Radius of gyration Rg (electron density) rg_electron26.99
Forward intensity I(0) i068341500.00
Molecular weight molecular_weight64820.0 kDa
Excluded volume excluded_volume81183 ų
Envelope volume envelope_volume100130 ų
Hydration-shell volume shell_volume31558 ų
Envelope diameter envelope_diameter97.9
Shell Rg shell_rg33.72
Envelope Rg envelope_rg26.93
Shape Rg shape_rg27.02
Total Rg total_rg27.59
Total atoms total_atoms4557
Residues n_residues581
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 dmax91.8
Rg (real space) rg_real27.76
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real6.8340e+07
I(0) uncertainty (real space) i0_real_error9.5880e+05
Rg (reciprocal space) rg_reciprocal27.77
I(0) (reciprocal space) i0_reciprocal68340000.0000
Solution quality estimate total_estimate0.8949
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha9478000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2wmob_
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 (3 domains)

Domain ID domain_id2wmoA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily410 — DOCK DHR2 domain, lobe A
Domain ID domain_id2wmoA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily740 — DOCK DHR2 domain, lobe C
Domain ID domain_id2wmoB00
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)