3wuv

Structure basis of inactivating cell abscission with chimera peptide 2

Method: X-RAY DIFFRACTION Dmax: 126.4 Å Quality: GOOD

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

Centrosomal protein of 55 kDa

Homo sapiens

UniProt Q53EZ4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 160–217 Chain B; UniProt 160–217 Fragment:UNP residues 160-217 peptide from Programmed cell death 6-interacting protein × 1 (Q8WUM4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 160–217 Chain E; UniProt 160–217 Fragment:UNP residues 160-217 peptide from Programmed cell death 6-interacting protein × 1 (Q8WUM4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 160–217 Chain H; UniProt 160–217 Fragment:UNP residues 160-217 peptide from Programmed cell death 6-interacting protein × 1 (Q8WUM4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 160–217 Chain K; UniProt 160–217 Fragment:UNP residues 160-217 peptide from Programmed cell death 6-interacting protein × 1 (Q8WUM4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 160–217 Chain N; UniProt 160–217 Fragment:UNP residues 160-217 peptide from Programmed cell death 6-interacting protein × 1 (Q8WUM4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
6 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 160–217 Chain Q; UniProt 160–217 Fragment:UNP residues 160-217 peptide from Programmed cell death 6-interacting protein × 1 (Q8WUM4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227

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.

3 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEP55_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–63; UniProt 160–217 Author chain B; PDBConstruct 6–63; UniProt 160–217 Author chain D; PDBConstruct 6–63; UniProt 160–217 Author chain E; PDBConstruct 6–63; UniProt 160–217 Author chain G; PDBConstruct 6–63; UniProt 160–217 Author chain H; PDBConstruct 6–63; UniProt 160–217 Author chain J; PDBConstruct 6–63; UniProt 160–217 Author chain K; PDBConstruct 6–63; UniProt 160–217 Author chain M; PDBConstruct 6–63; UniProt 160–217 Author chain N; PDBConstruct 6–63; UniProt 160–217 Author chain P; PDBConstruct 6–63; UniProt 160–217 Author chain Q; PDBConstruct 6–63; UniProt 160–217

peptide from Programmed cell death 6-interacting protein

OrganismNot specified

UniProt Q8WUM4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 796–809 Mutation:P796D/P807I/G808P/Y809P Centrosomal protein of 55 kDa × 2 (Q53EZ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 796–809 Mutation:P796D/P807I/G808P/Y809P Centrosomal protein of 55 kDa × 2 (Q53EZ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 796–809 Mutation:P796D/P807I/G808P/Y809P Centrosomal protein of 55 kDa × 2 (Q53EZ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain L; UniProt 796–809 Mutation:P796D/P807I/G808P/Y809P Centrosomal protein of 55 kDa × 2 (Q53EZ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
5 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain O; UniProt 796–809 Mutation:P796D/P807I/G808P/Y809P Centrosomal protein of 55 kDa × 2 (Q53EZ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227
6 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain R; UniProt 796–809 Mutation:P796D/P807I/G808P/Y809P Centrosomal protein of 55 kDa × 2 (Q53EZ4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;295 K;0.8M ammonium sulfate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.79 Å R-free 0.227

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.

18 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PDC6I_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–14; UniProt 796–809 Author chain F; PDBConstruct 1–14; UniProt 796–809 Author chain I; PDBConstruct 1–14; UniProt 796–809 Author chain L; PDBConstruct 1–14; UniProt 796–809 Author chain O; PDBConstruct 1–14; UniProt 796–809 Author chain R; PDBConstruct 1–14; UniProt 796–809

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 3wuv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3wuv
Deposition date deposition_date2014-05-05
Structure title titleStructure basis of inactivating cell abscission with chimera peptide 2
Keywords keywordsCoiled-coil, 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_guinier37.29
Radius of gyration Rg (electron density) rg_electron36.56
Forward intensity I(0) i0113914000.00
Molecular weight molecular_weight86899.0 kDa
Excluded volume excluded_volume109610 ų
Envelope volume envelope_volume166480 ų
Hydration-shell volume shell_volume39816 ų
Envelope diameter envelope_diameter136.1
Shell Rg shell_rg40.10
Envelope Rg envelope_rg37.06
Shape Rg shape_rg36.47
Total Rg total_rg37.14
Total atoms total_atoms6129
Residues n_residues749
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 dmax126.4
Rg (real space) rg_real37.32
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.1390e+08
I(0) uncertainty (real space) i0_real_error1.8850e+06
Rg (reciprocal space) rg_reciprocal37.31
I(0) (reciprocal space) i0_reciprocal113900000.0000
Solution quality estimate total_estimate0.8902
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.1
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.305
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7561000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id3wuvA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvG00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvH00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvJ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvK00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvM00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvN00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvP00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain
Domain ID domain_id3wuvQ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1180 — Geminin coiled-coil domain

8. Citations (1)

9. Files and Curves (10)