2yin

STRUCTURE OF THE COMPLEX BETWEEN Dock2 AND Rac1.

Method: X-RAY DIFFRACTION Dmax: 157.4 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1192–1622 Fragment:DHR2 DOMAIN, RESIDUES 1192-1622 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 (P63000) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;293 K;0.1 M MES PH 6.5, 12% (W/V) PEG 3350, 10% (V/V) GLYCEROL AND 150 MM NACL. AT 20 C Resolution 2.70 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1192–1622 Fragment:DHR2 DOMAIN, RESIDUES 1192-1622 RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 × 1 (P63000) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;293 K;0.1 M MES PH 6.5, 12% (W/V) PEG 3350, 10% (V/V) GLYCEROL AND 150 MM NACL. AT 20 C Resolution 2.70 Å R-free 0.255

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 6 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 6–436; UniProt 1192–1622 Author chain B; PDBConstruct 6–436; UniProt 1192–1622

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–177 Fragment:RESIDUES 1-177 DEDICATOR OF CYTOKINESIS PROTEIN 2 × 1 (Q92608) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;293 K;0.1 M MES PH 6.5, 12% (W/V) PEG 3350, 10% (V/V) GLYCEROL AND 150 MM NACL. AT 20 C Resolution 2.70 Å R-free 0.255
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–177 Fragment:RESIDUES 1-177 DEDICATOR OF CYTOKINESIS PROTEIN 2 × 1 (Q92608) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;293 K;0.1 M MES PH 6.5, 12% (W/V) PEG 3350, 10% (V/V) GLYCEROL AND 150 MM NACL. AT 20 C Resolution 2.70 Å R-free 0.255

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 101 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 C; PDBConstruct 20–196; UniProt 1–177 Author chain D; PDBConstruct 20–196; 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 2yin

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2yin
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2yin
Deposition date deposition_date2011-05-16
Structure title titleSTRUCTURE OF THE COMPLEX BETWEEN Dock2 AND Rac1.
Keywords keywordsAPOPTOSIS, DOCK, DOCK GUANINE NUCLEOTIDE EXCHANGE FACTORS, RHO GTPASE; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.05
Radius of gyration Rg (electron density) rg_electron42.68
Forward intensity I(0) i0264531000.00
Molecular weight molecular_weight135180.0 kDa
Excluded volume excluded_volume170140 ų
Envelope volume envelope_volume235750 ų
Hydration-shell volume shell_volume50327 ų
Envelope diameter envelope_diameter165.7
Shell Rg shell_rg43.03
Envelope Rg envelope_rg42.36
Shape Rg shape_rg42.71
Total Rg total_rg42.56
Total atoms total_atoms9525
Residues n_residues1182
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 dmax157.4
Rg (real space) rg_real42.58
Rg uncertainty (real space) rg_real_error2.02
I(0) (real space) i0_real2.6450e+08
I(0) uncertainty (real space) i0_real_error5.1750e+06
Rg (reciprocal space) rg_reciprocal42.06
I(0) (reciprocal space) i0_reciprocal264400000.0000
Solution quality estimate total_estimate0.7819
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.4
Skewness Skewness skewness0.727
Kurtosis Kurtosis kurtosis0.174
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37930000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.518; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.779; Smooth: 0.827

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2yinc1
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_idd2yinc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2yind1
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_idd2yind2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id2yinA01
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_id2yinA03
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_id2yinB01
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_id2yinB03
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_id2yinC00
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_id2yinD00
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)