1kzg

DbsCdc42(Y889F)

Method: X-RAY DIFFRACTION Dmax: 120.8 Å Quality: GOOD

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

GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS

Mus musculus

UniProt Q64096

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 A; UniProt 623–967 Fragment:DH/PH fragment (residues 623-967) Mutation:Y889F CDC42 HOMOLOG × 1 (P60953) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;PEG 8000,Tris HCL, NaFormate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.60 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 623–967 Fragment:DH/PH fragment (residues 623-967) Mutation:Y889F CDC42 HOMOLOG × 1 (P60953) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;PEG 8000,Tris HCL, NaFormate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.60 Å R-free 0.259

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.

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

View Construct and Data Evidence
UniProt name MCF2L_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–346; UniProt 623–967 Author chain C; PDBConstruct 2–346; UniProt 623–967

CDC42 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 B; UniProt 1–188 Fragment:residues 1-188 Mutation:C188S GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS × 1 (Q64096) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;PEG 8000,Tris HCL, NaFormate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.60 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–188 Fragment:residues 1-188 Mutation:C188S GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS × 1 (Q64096) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;291 K;PEG 8000,Tris HCL, NaFormate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.60 Å R-free 0.259

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 B; 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 1kzg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kzg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1kzg
Deposition date deposition_date2002-02-06
Structure title titleDbsCdc42(Y889F)
Keywords keywordsguanine nucleotide exchange factor, small G-protein, Cdc42, Dbs, DH/PH, 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_guinier36.37
Radius of gyration Rg (electron density) rg_electron35.84
Forward intensity I(0) i0208616000.00
Molecular weight molecular_weight117940.0 kDa
Excluded volume excluded_volume148340 ų
Envelope volume envelope_volume199500 ų
Hydration-shell volume shell_volume46694 ų
Envelope diameter envelope_diameter122.2
Shell Rg shell_rg42.14
Envelope Rg envelope_rg34.88
Shape Rg shape_rg35.83
Total Rg total_rg36.33
Total atoms total_atoms8281
Residues n_residues1032
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 dmax120.8
Rg (real space) rg_real36.35
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real2.0860e+08
I(0) uncertainty (real space) i0_real_error3.5290e+06
Rg (reciprocal space) rg_reciprocal36.36
I(0) (reciprocal space) i0_reciprocal208600000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.1
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.430
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19610000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1kzga1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1kzga2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1kzgb_
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_idd1kzgc1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd1kzgc2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)
Domain ID domain_idd1kzgd_
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_id1kzgA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1kzgA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1kzgB00
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_id1kzgC01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id1kzgC02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id1kzgD00
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)