2qrz

Cdc42 bound to GMP-PCP: Induced Fit by Effector is Required

Method: X-RAY DIFFRACTION Dmax: 76.1 Å Quality: EXCELLENT

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

Cell division control protein 42 homolog precursor

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–189 Chain B; UniProt 1–189 Not recorded MG MAGNESIUM ION × 2 SO4 SULFATE ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;12% PEG 6K, 100 mM Na Acetate, 50 mM MES, pH 6.0, 100 mM Ammonium Sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.40 Å R-free 0.263

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 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC42_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–189; UniProt 1–189 Author chain B; PDBConstruct 1–189; UniProt 1–189

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 2qrz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2qrz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2qrz
Deposition date deposition_date2007-07-30
Structure title titleCdc42 bound to GMP-PCP: Induced Fit by Effector is Required
Keywords keywords;G-domain fold, G protein, GTPase, Alternative splicing, GTP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Prenylation, CELL CYCLE ;; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.67
Radius of gyration Rg (electron density) rg_electron22.70
Forward intensity I(0) i030864400.00
Molecular weight molecular_weight42893.0 kDa
Excluded volume excluded_volume53857 ų
Envelope volume envelope_volume65422 ų
Hydration-shell volume shell_volume24088 ų
Envelope diameter envelope_diameter79.0
Shell Rg shell_rg29.60
Envelope Rg envelope_rg22.90
Shape Rg shape_rg22.70
Total Rg total_rg23.55
Total atoms total_atoms3002
Residues n_residues375
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 dmax76.1
Rg (real space) rg_real23.63
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real3.0860e+07
I(0) uncertainty (real space) i0_real_error4.0990e+05
Rg (reciprocal space) rg_reciprocal23.64
I(0) (reciprocal space) i0_reciprocal30860000.0000
Solution quality estimate total_estimate0.9019
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.464
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5663000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2qrza_
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_idd2qrzb_
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 (2 domains)

Domain ID domain_id2qrzA00
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_id2qrzB00
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)