1e0a

Cdc42 complexed with the GTPase binding domain of p21 activated kinase

Method: SOLUTION NMR Dmax: 63.8 Å Quality: REASONABLE

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

Cell division control protein 42 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 A; UniProt 1–184 Fragment:1-184 Mutation:YES Serine/threonine-protein kinase PAK 1 × 1 (P35465) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SOLUTION NMR NMR measurement conditions:pH 5.5;298 K;Ionic strength (raw mmCIF value) 5 MM NA2HPO4, 25MM NACL;Pressure 1 NMR sample composition:90% WATER, 10% D2O 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 1–184; UniProt 1–184

Serine/threonine-protein kinase PAK 1

Rattus norvegicus

UniProt P35465

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 75–118 Fragment:75-118 Mutation:YES Cell division control protein 42 homolog × 1 (P60953) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SOLUTION NMR NMR measurement conditions:pH 5.5;298 K;Ionic strength (raw mmCIF value) 5 MM NA2HPO4, 25MM NACL;Pressure 1 NMR sample composition:90% WATER, 10% D2O 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PAK1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–46; UniProt 75–118

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 1e0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e0a
Deposition date deposition_date2000-03-16
Structure title titleCdc42 complexed with the GTPase binding domain of p21 activated kinase
Keywords keywordsSIGNALLING PROTEIN, G PROTEIN SIGNALLING SER/THR KINASE, SIGNALLING PROTEIN-KINASE COMPLEX; SIGNALLING PROTEIN/KINASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.21
Radius of gyration Rg (electron density) rg_electron18.05
Forward intensity I(0) i03648390000.00
Molecular weight molecular_weight520950.0 kDa
Excluded volume excluded_volume654240 ų
Envelope volume envelope_volume67071 ų
Hydration-shell volume shell_volume25331 ų
Envelope diameter envelope_diameter74.9
Shell Rg shell_rg29.59
Envelope Rg envelope_rg22.57
Shape Rg shape_rg18.02
Total Rg total_rg18.33
Total atoms total_atoms72980
Residues n_residues4600
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 dmax63.8
Rg (real space) rg_real18.17
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real3.6480e+09
I(0) uncertainty (real space) i0_real_error4.4030e+07
Rg (reciprocal space) rg_reciprocal18.18
I(0) (reciprocal space) i0_reciprocal3648000000.0000
Solution quality estimate total_estimate0.6222
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.302
Kurtosis Kurtosis kurtosis-0.227
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1539000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.703; Stabil: 0.998; Sysdev: 0.330; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1e0aa_
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_idd1e0ab1
Class classj — Peptides
Fold Fold foldj.65 — Peptide derived from p-21 activated kinase
Superfamily Superfamily superfamilyj.65.1 — Peptide derived from p-21 activated kinase
Family Family familyj.65.1.1 — Peptide derived from p-21 activated kinase
Domain ID domain_idd1e0ab2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1e0aA00
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_id1e0aB00
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)