3gcg

crystal structure of MAP and CDC42 complex

Method: X-RAY DIFFRACTION Dmax: 66.8 Å Quality: GOOD

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 2–178 Fragment:UNP residues 2-178 L0028 (Mitochondria associated protein) × 1 (Q9R8E4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;0.1M Hepes pH 7.5, 10% PEG 6000, 5% MPD, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.30 Å R-free 0.277

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 6–182; UniProt 2–178

L0028 (Mitochondria associated protein)

Escherichia coli

UniProt Q9R8E4

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 37–203 Fragment:UNP residues 37-203 Cell division control protein 42 homolog × 1 (P60953) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;0.1M Hepes pH 7.5, 10% PEG 6000, 5% MPD, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.30 Å R-free 0.277

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 Q9R8E4_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–172; UniProt 37–203

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 3gcg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3gcg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3gcg
Deposition date deposition_date2009-02-22
Structure title titlecrystal structure of MAP and CDC42 complex
Keywords keywords;MAP, CDC42, COMPLEX, Alternative splicing, Cell membrane, GTP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Prenylation cdc42, SIGNALING PROTEIN-TRANSCRIPTION COMPLEX ;; SIGNALING PROTEIN/TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.21
Radius of gyration Rg (electron density) rg_electron20.21
Forward intensity I(0) i023197000.00
Molecular weight molecular_weight36670.0 kDa
Excluded volume excluded_volume45949 ų
Envelope volume envelope_volume54482 ų
Hydration-shell volume shell_volume22284 ų
Envelope diameter envelope_diameter72.9
Shell Rg shell_rg26.89
Envelope Rg envelope_rg20.43
Shape Rg shape_rg20.18
Total Rg total_rg21.19
Total atoms total_atoms2581
Residues n_residues325
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 dmax66.8
Rg (real space) rg_real21.07
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real2.3200e+07
I(0) uncertainty (real space) i0_real_error2.9770e+05
Rg (reciprocal space) rg_reciprocal21.10
I(0) (reciprocal space) i0_reciprocal23200000.0000
Solution quality estimate total_estimate0.8215
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.126
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5600000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3gcga_
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_id3gcgA00
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_id3gcgB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology4120 — SopE-like GEF fold
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)