9lx0

DOCK5/ELMO1 complex with RhoG and Rac1 on lipid membrane

Method: ELECTRON MICROSCOPY Dmax: 277.8 Å Quality: EXCELLENT

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

Engulfment and cell motility protein 1

Homo sapiens

UniProt Q92556

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 1–727 Chain E; UniProt 1–727 Not recorded Dedicator of cytokinesis protein 5 × 2 (Q9H7D0) Rho-related GTP-binding protein RhoG × 2 (P84095) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.98 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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELMO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–733; UniProt 1–727 Author chain E; PDBConstruct 7–733; UniProt 1–727

Dedicator of cytokinesis protein 5

Homo sapiens

UniProt Q9H7D0

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 1–1870 Chain F; UniProt 1–1870 Not recorded Engulfment and cell motility protein 1 × 2 (Q92556) Rho-related GTP-binding protein RhoG × 2 (P84095) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.98 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DOCK5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–1876; UniProt 1–1870 Author chain F; PDBConstruct 7–1876; UniProt 1–1870

Rho-related GTP-binding protein RhoG

Homo sapiens

UniProt P84095

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 C; UniProt 1–191 Chain G; UniProt 1–191 Mutation:Q61L Engulfment and cell motility protein 1 × 2 (Q92556) Dedicator of cytokinesis protein 5 × 2 (Q9H7D0) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.98 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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOG_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 8–198; UniProt 1–191 Author chain G; PDBConstruct 8–198; UniProt 1–191

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 D; UniProt 1–188 Chain H; UniProt 1–188 Mutation:G15A, C189S Engulfment and cell motility protein 1 × 2 (Q92556) Dedicator of cytokinesis protein 5 × 2 (Q9H7D0) Rho-related GTP-binding protein RhoG × 2 (P84095) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.98 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 4
Chains and sequence ranges Author chain D; PDBConstruct 8–195; UniProt 1–188 Author chain H; 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 9lx0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9lx0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9lx0
Deposition date deposition_date2025-02-17
Structure title titleDOCK5/ELMO1 complex with RhoG and Rac1 on lipid membrane
Keywords keywordsComplex, Rho-GTPase, GEF, Lipid membrane, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron103.10
Forward intensity I(0) i05193210000.00
Molecular weight molecular_weight626760.0 kDa
Excluded volume excluded_volume790210 ų
Envelope volume envelope_volume1680300 ų
Hydration-shell volume shell_volume146170 ų
Envelope diameter envelope_diameter335.8
Shell Rg shell_rg80.26
Envelope Rg envelope_rg98.99
Shape Rg shape_rg103.10
Total Rg total_rg103.00
Total atoms total_atoms44082
Residues n_residues5452
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 dmax277.8
Rg (real space) rg_real97.87
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real5.0250e+09
I(0) uncertainty (real space) i0_real_error1.0700e+08
Rg (reciprocal space) rg_reciprocal93.52
I(0) (reciprocal space) i0_reciprocal5055000000.0000
Solution quality estimate total_estimate0.9125
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.6
Skewness Skewness skewness0.413
Kurtosis Kurtosis kurtosis-0.736
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.4186
Highest regularization parameter α highest_alpha198300000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 0.955; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.147

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)