7dpa

Cryo-EM structure of the human ELMO1-DOCK5-Rac1 complex

Method: ELECTRON MICROSCOPY Dmax: 228.3 Å Quality: GOOD

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

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1642 Chain D; UniProt 1–1642 Not recorded Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) Engulfment and cell motility protein 1 × 2 (Q92556) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 1
Chains and sequence ranges Author chain A; PDBConstruct 7–1648; UniProt 1–1642 Author chain D; PDBConstruct 7–1648; UniProt 1–1642

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–177 Chain E; UniProt 1–177 Mutation:G15A Dedicator of cytokinesis protein 5 × 2 (Q9H7D0) Engulfment and cell motility protein 1 × 2 (Q92556) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 E; PDBConstruct 8–184; UniProt 1–177

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–727 Chain F; UniProt 1–727 Not recorded Dedicator of cytokinesis protein 5 × 2 (Q9H7D0) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 3
Chains and sequence ranges Author chain C; PDBConstruct 7–733; UniProt 1–727 Author chain F; PDBConstruct 7–733; UniProt 1–727

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 7dpa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7dpa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7dpa
Deposition date deposition_date2020-12-18
Structure title titleCryo-EM structure of the human ELMO1-DOCK5-Rac1 complex
Keywords keywordsELMO, DOCK, GEF, GTPASE, RHO, RAC, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier78.77
Radius of gyration Rg (electron density) rg_electron79.03
Forward intensity I(0) i02867360000.00
Molecular weight molecular_weight466890.0 kDa
Excluded volume excluded_volume589760 ų
Envelope volume envelope_volume1133600 ų
Hydration-shell volume shell_volume124320 ų
Envelope diameter envelope_diameter245.8
Shell Rg shell_rg76.01
Envelope Rg envelope_rg73.86
Shape Rg shape_rg79.01
Total Rg total_rg79.03
Total atoms total_atoms32858
Residues n_residues4034
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 dmax228.3
Rg (real space) rg_real78.95
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real2.8670e+09
I(0) uncertainty (real space) i0_real_error5.6110e+07
Rg (reciprocal space) rg_reciprocal77.66
I(0) (reciprocal space) i0_reciprocal2858000000.0000
Solution quality estimate total_estimate0.8446
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary91.3
Skewness Skewness skewness0.255
Kurtosis Kurtosis kurtosis-0.755
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0063
Highest regularization parameter α highest_alpha96920000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)