6tky

Crystal structure of the DHR2 domain of DOCK10 in complex with CDC42

Method: X-RAY DIFFRACTION Dmax: 114.7 Å Quality: EXCELLENT

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

Dedicator of cytokinesis protein 10

Homo sapiens

UniProt Q96BY6

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 1694–2150 Not recorded Cell division control protein 42 homolog × 1 (P60953) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.5;293 K;25% (w/v) PEG 3350, 200 mM potassium acetate, 8% (v/v) 1,1,1,3,3,3-Hexafluoro-2-propanol. Resolution 2.55 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1694–2151 Not recorded Cell division control protein 42 homolog × 1 (P60953) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.5;293 K;25% (w/v) PEG 3350, 200 mM potassium acetate, 8% (v/v) 1,1,1,3,3,3-Hexafluoro-2-propanol. Resolution 2.55 Å R-free 0.246

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.

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

View Construct and Data Evidence
UniProt name DOC10_HUMAN
Isoform
PDB entities 1, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–457; UniProt 1694–2150 Author chain A; PDBConstruct 1–458; UniProt 1694–2151

Cell division control protein 42 homolog

Homo sapiens

UniProt P60953

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 D; UniProt 1–188 Not recorded Dedicator of cytokinesis protein 10 × 1 (Q96BY6) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.5;293 K;25% (w/v) PEG 3350, 200 mM potassium acetate, 8% (v/v) 1,1,1,3,3,3-Hexafluoro-2-propanol. Resolution 2.55 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–188 Not recorded Dedicator of cytokinesis protein 10 × 1 (Q96BY6) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7.5;293 K;25% (w/v) PEG 3350, 200 mM potassium acetate, 8% (v/v) 1,1,1,3,3,3-Hexafluoro-2-propanol. Resolution 2.55 Å R-free 0.246

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.

45 other PDB entries and 67 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC42_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–188; UniProt 1–188 Author chain D; PDBConstruct 1–188; 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 6tky

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6tky
Deposition date deposition_date2019-11-29
Structure title titleCrystal structure of the DHR2 domain of DOCK10 in complex with CDC42
Keywords keywordsDOCK10 GEF CDC42 GTPase, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.41
Radius of gyration Rg (electron density) rg_electron35.80
Forward intensity I(0) i0256192000.00
Molecular weight molecular_weight132120.0 kDa
Excluded volume excluded_volume166390 ų
Envelope volume envelope_volume216870 ų
Hydration-shell volume shell_volume50291 ų
Envelope diameter envelope_diameter118.9
Shell Rg shell_rg42.25
Envelope Rg envelope_rg35.27
Shape Rg shape_rg35.81
Total Rg total_rg36.24
Total atoms total_atoms9312
Residues n_residues1188
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 dmax114.7
Rg (real space) rg_real36.27
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real2.5620e+08
I(0) uncertainty (real space) i0_real_error4.1900e+06
Rg (reciprocal space) rg_reciprocal36.36
I(0) (reciprocal space) i0_reciprocal256200000.0000
Solution quality estimate total_estimate0.9060
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.3
Skewness Skewness skewness0.151
Kurtosis Kurtosis kurtosis-0.598
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33460000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6tkyc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd6tkyd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (6 domains)

Domain ID domain_id6tkyA01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily410 — DOCK DHR2 domain, lobe A
Domain ID domain_id6tkyA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily740 — DOCK DHR2 domain, lobe C
Domain ID domain_id6tkyB01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily410 — DOCK DHR2 domain, lobe A
Domain ID domain_id6tkyB03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily740 — DOCK DHR2 domain, lobe C
Domain ID domain_id6tkyC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6tkyD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)