5vzu

Crystal structure of the Skp1-FBXO31-cyclin D1 complex

Method: X-RAY DIFFRACTION Dmax: 145.8 Å Quality: GOOD

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

S-phase kinase-associated protein 1

Homo sapiens

UniProt P63208

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 1–163 Mutation:P2A F-box only protein 31 × 1 (Q5XUX0) Cyclin D1 × 1 (Q9H014) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;277 K;100 mM sodium citrate (pH 5.3), 0.27 M ammonium acetate, 13-17% MPD, 0.02 M CaCl2 Resolution 2.70 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–163 Mutation:P2A F-box only protein 31 × 1 (Q5XUX0) Cyclin D1 × 1 (Q9H014) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;277 K;100 mM sodium citrate (pH 5.3), 0.27 M ammonium acetate, 13-17% MPD, 0.02 M CaCl2 Resolution 2.70 Å R-free 0.233

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.

71 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–149; UniProt 1–163 Author chain C; PDBConstruct 1–149; UniProt 1–163

F-box only protein 31

Homo sapiens

UniProt Q5XUX0

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 B; UniProt 66–539 Not recorded S-phase kinase-associated protein 1 × 1 (P63208) Cyclin D1 × 1 (Q9H014) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;277 K;100 mM sodium citrate (pH 5.3), 0.27 M ammonium acetate, 13-17% MPD, 0.02 M CaCl2 Resolution 2.70 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 66–539 Not recorded S-phase kinase-associated protein 1 × 1 (P63208) Cyclin D1 × 1 (Q9H014) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;277 K;100 mM sodium citrate (pH 5.3), 0.27 M ammonium acetate, 13-17% MPD, 0.02 M CaCl2 Resolution 2.70 Å R-free 0.233

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FBX31_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 15–488; UniProt 66–539 Author chain D; PDBConstruct 15–488; UniProt 66–539

Cyclin D1

OrganismNot specified

UniProt Q9H014

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 E; UniProt 109–125 Fragment:UNP residues 109-125 Non-standard monomer:Yes (specific site not provided by mmCIF) S-phase kinase-associated protein 1 × 1 (P63208) F-box only protein 31 × 1 (Q5XUX0) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;277 K;100 mM sodium citrate (pH 5.3), 0.27 M ammonium acetate, 13-17% MPD, 0.02 M CaCl2 Resolution 2.70 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 109–125 Fragment:UNP residues 109-125 Non-standard monomer:Yes (specific site not provided by mmCIF) S-phase kinase-associated protein 1 × 1 (P63208) F-box only protein 31 × 1 (Q5XUX0) ZN ZINC ION × 1 PO4 PHOSPHATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.3;277 K;100 mM sodium citrate (pH 5.3), 0.27 M ammonium acetate, 13-17% MPD, 0.02 M CaCl2 Resolution 2.70 Å R-free 0.233

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 Q9H014_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–17; UniProt 109–125 Author chain F; PDBConstruct 1–17; UniProt 109–125

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 5vzu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vzu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vzu
Deposition date deposition_date2017-05-29
Structure title titleCrystal structure of the Skp1-FBXO31-cyclin D1 complex
Keywords keywordsubiquitin ligase, 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_guinier46.31
Radius of gyration Rg (electron density) rg_electron46.24
Forward intensity I(0) i0262571000.00
Molecular weight molecular_weight131570.0 kDa
Excluded volume excluded_volume163870 ų
Envelope volume envelope_volume251790 ų
Hydration-shell volume shell_volume46264 ų
Envelope diameter envelope_diameter147.8
Shell Rg shell_rg50.45
Envelope Rg envelope_rg44.37
Shape Rg shape_rg46.22
Total Rg total_rg46.52
Total atoms total_atoms9243
Residues n_residues1138
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 dmax145.8
Rg (real space) rg_real46.38
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real2.6260e+08
I(0) uncertainty (real space) i0_real_error5.0550e+06
Rg (reciprocal space) rg_reciprocal46.31
I(0) (reciprocal space) i0_reciprocal262500000.0000
Solution quality estimate total_estimate0.8497
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.3
Skewness Skewness skewness0.186
Kurtosis Kurtosis kurtosis-0.742
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13590000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.279

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5vzuA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id5vzuC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A

8. Citations (1)

9. Files and Curves (10)