1aje

CDC42 FROM HUMAN, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 66.4 Å Quality: GOOD

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

CDC42HS

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–187 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;298 K 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 8–194; UniProt 1–187

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 1aje

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1aje
Deposition date deposition_date1997-05-02
Structure title titleCDC42 FROM HUMAN, NMR, 20 STRUCTURES
Keywords keywordsG-PROTEIN, CELLULAR SIGNALING, CYTOSKELETAL REARRANGEMENT; G-PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.81
Radius of gyration Rg (electron density) rg_electron17.47
Forward intensity I(0) i02343420000.00
Molecular weight molecular_weight429740.0 kDa
Excluded volume excluded_volume545530 ų
Envelope volume envelope_volume71056 ų
Hydration-shell volume shell_volume25981 ų
Envelope diameter envelope_diameter74.7
Shell Rg shell_rg30.27
Envelope Rg envelope_rg23.47
Shape Rg shape_rg17.43
Total Rg total_rg17.81
Total atoms total_atoms61060
Residues n_residues3880
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 dmax66.4
Rg (real space) rg_real17.84
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real2.3430e+09
I(0) uncertainty (real space) i0_real_error2.8580e+07
Rg (reciprocal space) rg_reciprocal17.83
I(0) (reciprocal space) i0_reciprocal2343000000.0000
Solution quality estimate total_estimate0.8205
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.7
Skewness Skewness skewness0.457
Kurtosis Kurtosis kurtosis0.042
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2037000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.594; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.896; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ajea1
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_idd1ajea2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1ajeA00
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)