3b13

Crystal structure of the DHR-2 domain of DOCK2 in complex with Rac1 (T17N mutant)

Method: X-RAY DIFFRACTION Dmax: 151.0 Å Quality: GOOD

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1196–1622 Chain C; UniProt 1196–1622 Fragment:DHR-2 domain (UNP RESIDUES 1196-1622) Ras-related C3 botulinum toxin substrate 1 × 2 (P63000) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;100mM sodium citrate, 15% PEG 6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.01 Å R-free 0.234

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 5–431; UniProt 1196–1622 Author chain C; PDBConstruct 5–431; UniProt 1196–1622

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–177 Chain D; UniProt 1–177 Fragment:GTPase domain (UNP RESIDUES 1-177) Mutation:T17N Dedicator of cytokinesis protein 2 × 2 (Q92608) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;293 K;100mM sodium citrate, 15% PEG 6000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.01 Å R-free 0.234

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

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 3b13

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3b13
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3b13
Deposition date deposition_date2011-06-24
Structure title titleCrystal structure of the DHR-2 domain of DOCK2 in complex with Rac1 (T17N mutant)
Keywords keywords;protein-ptotein complex, lymphocyte chemotaxis, signal tansduction, guanine nucleotide exchange factor, GTPase, PROTEIN BINDING-SIGNALING PROTEIN complex ;; PROTEIN BINDING/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.04
Radius of gyration Rg (electron density) rg_electron44.06
Forward intensity I(0) i0284765000.00
Molecular weight molecular_weight140690.0 kDa
Excluded volume excluded_volume176800 ų
Envelope volume envelope_volume243180 ų
Hydration-shell volume shell_volume47604 ų
Envelope diameter envelope_diameter164.3
Shell Rg shell_rg46.45
Envelope Rg envelope_rg43.59
Shape Rg shape_rg44.04
Total Rg total_rg44.24
Total atoms total_atoms9898
Residues n_residues1208
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 dmax151.0
Rg (real space) rg_real44.34
Rg uncertainty (real space) rg_real_error2.15
I(0) (real space) i0_real2.8480e+08
I(0) uncertainty (real space) i0_real_error5.8030e+06
Rg (reciprocal space) rg_reciprocal44.05
I(0) (reciprocal space) i0_reciprocal284700000.0000
Solution quality estimate total_estimate0.8383
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.8
Skewness Skewness skewness0.412
Kurtosis Kurtosis kurtosis-0.638
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30800000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.751; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.778; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3b13b_
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_idd3b13d_
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_id3b13A01
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_id3b13A03
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_id3b13B00
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_id3b13C01
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_id3b13C03
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_id3b13D00
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)