1cee

SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP

Method: SOLUTION NMR Dmax: 49.2 Å Quality: REASONABLE

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

GTP-BINDING RHO-LIKE PROTEIN

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 A; UniProt 1–179 Fragment:CDC42 WISKOTT-ALDRICH SYNDROME PROTEIN WASP × 1 (P42768) MG MAGNESIUM ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 50mM;Pressure 1 Resolution not provided

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 1–179; UniProt 1–179

WISKOTT-ALDRICH SYNDROME PROTEIN WASP

Homo sapiens

UniProt P42768

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 230–288 Fragment:GTPASE BINDING DOMAIN OF WASP GTP-BINDING RHO-LIKE PROTEIN × 1 (P60953) MG MAGNESIUM ION × 1 GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER × 1 SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 50mM;Pressure 1 Resolution not provided

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WASP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–59; UniProt 230–288

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 1cee

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cee
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cee
Deposition date deposition_date1999-03-08
Structure title titleSOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING DOMAIN OF WASP
Keywords keywordsCDC42 ACTIN REGULATOR GTPASE AND THE GTPASE BINDING DOMAIN OF ITS EFFECTOR WASP, Structural protein Regulation; Structural protein Regulation
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.92
Radius of gyration Rg (electron density) rg_electron18.57
Forward intensity I(0) i03926820000.00
Molecular weight molecular_weight535490.0 kDa
Excluded volume excluded_volume670900 ų
Envelope volume envelope_volume89200 ų
Hydration-shell volume shell_volume30452 ų
Envelope diameter envelope_diameter84.1
Shell Rg shell_rg32.06
Envelope Rg envelope_rg24.98
Shape Rg shape_rg18.54
Total Rg total_rg18.86
Total atoms total_atoms75020
Residues n_residues4760
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 dmax49.2
Rg (real space) rg_real18.01
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real3.7450e+09
I(0) uncertainty (real space) i0_real_error3.2240e+07
Rg (reciprocal space) rg_reciprocal18.92
I(0) (reciprocal space) i0_reciprocal3927000000.0000
Solution quality estimate total_estimate0.6846
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha2.3900
Highest regularization parameter α highest_alpha3848000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.986; Stabil: 0.984; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ceea_
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_id1ceeA00
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_id1ceeB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology810 — SerineThreonine-protein kinase PAK-alpha; Chain A
Homologous superfamily homologous superfamily10 — CRIB domain

8. Citations (1)

9. Files and Curves (10)