6tgc

CryoEM structure of the ternary DOCK2-ELMO1-RAC1 complex.

Method: ELECTRON MICROSCOPY Dmax: 255.5 Å Quality: EXCELLENT

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

Dedicator of cytokinesis protein 2

Homo sapiens

UniProt Q92608

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 1–1830 Chain D; UniProt 1–1830 Not recorded Engulfment and cell motility protein 1 × 2 (Q92556) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DOCK2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1830; UniProt 1–1830 Author chain D; PDBConstruct 1–1830; UniProt 1–1830

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 B; UniProt 1–727 Chain E; UniProt 1–727 Not recorded Dedicator of cytokinesis protein 2 × 2 (Q92608) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–727; UniProt 1–727 Author chain E; PDBConstruct 1–727; UniProt 1–727

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 C; UniProt 1–192 Chain F; UniProt 1–192 Not recorded Dedicator of cytokinesis protein 2 × 2 (Q92608) Engulfment and cell motility protein 1 × 2 (Q92556) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–192; UniProt 1–192 Author chain F; PDBConstruct 1–192; UniProt 1–192

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 6tgc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6tgc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6tgc
Deposition date deposition_date2019-11-15
Structure title titleCryoEM structure of the ternary DOCK2-ELMO1-RAC1 complex.
Keywords keywordsguanine nucleotide exchange factor, cytoskeleton, actin, cryoEM, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier92.11
Radius of gyration Rg (electron density) rg_electron93.70
Forward intensity I(0) i03114750000.00
Molecular weight molecular_weight471450.0 kDa
Excluded volume excluded_volume587990 ų
Envelope volume envelope_volume1211400 ų
Hydration-shell volume shell_volume116650 ų
Envelope diameter envelope_diameter335.3
Shell Rg shell_rg74.76
Envelope Rg envelope_rg91.73
Shape Rg shape_rg93.75
Total Rg total_rg93.27
Total atoms total_atoms33282
Residues n_residues4614
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 dmax255.5
Rg (real space) rg_real87.63
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real2.9940e+09
I(0) uncertainty (real space) i0_real_error5.9250e+07
Rg (reciprocal space) rg_reciprocal86.18
I(0) (reciprocal space) i0_reciprocal3058000000.0000
Solution quality estimate total_estimate0.9102
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary90.2
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.649
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha0.8772
Highest regularization parameter α highest_alpha99780000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 0.975; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)