9vm7

Structure of DOCK6 tetramer complexed with Rac1

Method: ELECTRON MICROSCOPY Dmax: 278.5 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–2047 Chain C; UniProt 1–2047 Chain E; UniProt 1–2047 Chain G; UniProt 1–2047 Not recorded Ras-related C3 botulinum toxin substrate 1 × 4 (P63000) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 6.85 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 Author chain C; PDBConstruct 7–2053; UniProt 1–2047 Author chain E; PDBConstruct 7–2053; UniProt 1–2047 Author chain G; 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–177 Chain D; UniProt 1–177 Chain F; UniProt 1–177 Chain H; UniProt 1–177 Mutation:G15A Dedicator of cytokinesis protein 6 × 4 (Q96HP0) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 6.85 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 Author chain D; PDBConstruct 8–184; UniProt 1–177 Author chain F; PDBConstruct 8–184; UniProt 1–177 Author chain H; 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 9vm7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vm7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vm7
Deposition date deposition_date2025-06-27
Structure title titleStructure of DOCK6 tetramer complexed with Rac1
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_guinier73.03
Radius of gyration Rg (electron density) rg_electron72.30
Forward intensity I(0) i09459490000.00
Molecular weight molecular_weight843090.0 kDa
Excluded volume excluded_volume1062100 ų
Envelope volume envelope_volume1843400 ų
Hydration-shell volume shell_volume210000 ų
Envelope diameter envelope_diameter223.0
Shell Rg shell_rg79.93
Envelope Rg envelope_rg66.65
Shape Rg shape_rg72.28
Total Rg total_rg72.48
Total atoms total_atoms59424
Residues n_residues7460
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 dmax278.5
Rg (real space) rg_real77.07
Rg uncertainty (real space) rg_real_error1.94
I(0) (real space) i0_real9.5230e+09
I(0) uncertainty (real space) i0_real_error1.9290e+08
Rg (reciprocal space) rg_reciprocal74.03
I(0) (reciprocal space) i0_reciprocal9484000000.0000
Solution quality estimate total_estimate0.8639
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.8
Skewness Skewness skewness0.588
Kurtosis Kurtosis kurtosis0.759
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.8320
Highest regularization parameter α highest_alpha500700000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.587; Stabil: 0.863; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)