9vm4

Structure of DOCK6-Rac1 complex protomer

Method: ELECTRON MICROSCOPY Dmax: 176.3 Å Quality: GOOD

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

Dedicator of cytokinesis protein 6

Homo sapiens

UniProt Q96HP0

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 1–2047 Not recorded Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 4.20 Å

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DOCK6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–2053; UniProt 1–2047

Ras-related C3 botulinum toxin substrate 1

Homo sapiens

UniProt P63000

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 1–177 Mutation:G15A Dedicator of cytokinesis protein 6 × 1 (Q96HP0) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 4.20 Å

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.

74 other PDB entries and 102 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 8–184; UniProt 1–177

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 9vm4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vm4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vm4
Deposition date deposition_date2025-06-27
Structure title titleStructure of DOCK6-Rac1 complex protomer
Keywords keywordsDOCK, GEF, Rho, small GTPase, Rac, Cdc42, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.86
Radius of gyration Rg (electron density) rg_electron53.83
Forward intensity I(0) i0614549000.00
Molecular weight molecular_weight210770.0 kDa
Excluded volume excluded_volume265540 ų
Envelope volume envelope_volume402170 ų
Hydration-shell volume shell_volume64297 ų
Envelope diameter envelope_diameter177.6
Shell Rg shell_rg55.59
Envelope Rg envelope_rg51.31
Shape Rg shape_rg53.84
Total Rg total_rg53.86
Total atoms total_atoms14856
Residues n_residues1865
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 dmax176.3
Rg (real space) rg_real53.99
Rg uncertainty (real space) rg_real_error2.03
I(0) (real space) i0_real6.1450e+08
I(0) uncertainty (real space) i0_real_error1.1860e+07
Rg (reciprocal space) rg_reciprocal53.71
I(0) (reciprocal space) i0_reciprocal614300000.0000
Solution quality estimate total_estimate0.8434
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.5
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.852
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51050000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.903; Smooth: 0.525

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)