3v7d

Crystal Structure of ScSkp1-ScCdc4-pSic1 peptide complex

Method: X-RAY DIFFRACTION Dmax: 140.6 Å Quality: GOOD

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

Suppressor of kinetochore protein 1

Saccharomyces cerevisiae

UniProt P52286

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 1–194 Not recorded Cell division control protein 4 × 1 (P07834) Protein SIC1 × 1 (P38634) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;1.5 M Ammonium Sulphate, 0.1 M Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.31 Å R-free 0.221
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–194 Not recorded Cell division control protein 4 × 1 (P07834) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;1.5 M Ammonium Sulphate, 0.1 M Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.31 Å R-free 0.221

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.

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–169; UniProt 1–194 Author chain C; PDBConstruct 4–169; UniProt 1–194

Cell division control protein 4

Saccharomyces cerevisiae

UniProt P07834

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 263–744 Fragment:UNP residues 263-744 Mutation:C608L Suppressor of kinetochore protein 1 × 1 (P52286) Protein SIC1 × 1 (P38634) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;1.5 M Ammonium Sulphate, 0.1 M Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.31 Å R-free 0.221
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 263–744 Fragment:UNP residues 263-744 Mutation:C608L Suppressor of kinetochore protein 1 × 1 (P52286) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;1.5 M Ammonium Sulphate, 0.1 M Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.31 Å R-free 0.221

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–464; UniProt 263–744 Author chain D; PDBConstruct 3–464; UniProt 263–744

Protein SIC1

OrganismNot specified

UniProt P38634

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 67–85 Fragment:UNP residues 67-85 Non-standard monomer:Yes (specific site not provided by mmCIF) Suppressor of kinetochore protein 1 × 1 (P52286) Cell division control protein 4 × 1 (P07834) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;1.5 M Ammonium Sulphate, 0.1 M Hepes, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.31 Å R-free 0.221

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.

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

View Construct and Data Evidence
UniProt name SIC1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–19; UniProt 67–85

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 3v7d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3v7d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3v7d
Deposition date deposition_date2011-12-20
Structure title titleCrystal Structure of ScSkp1-ScCdc4-pSic1 peptide complex
Keywords keywordsWD 40 domain, phospho-peptide complex, E3 ubiquitin ligase, ligase, cell cycle, phospho binding protein, Sic1, phosphorylation; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.98
Radius of gyration Rg (electron density) rg_electron43.62
Forward intensity I(0) i0267262000.00
Molecular weight molecular_weight135720.0 kDa
Excluded volume excluded_volume170680 ų
Envelope volume envelope_volume242080 ų
Hydration-shell volume shell_volume47994 ų
Envelope diameter envelope_diameter137.3
Shell Rg shell_rg46.87
Envelope Rg envelope_rg42.13
Shape Rg shape_rg43.61
Total Rg total_rg43.83
Total atoms total_atoms9574
Residues n_residues1183
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 dmax140.6
Rg (real space) rg_real44.09
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real2.6730e+08
I(0) uncertainty (real space) i0_real_error4.8210e+06
Rg (reciprocal space) rg_reciprocal43.98
I(0) (reciprocal space) i0_reciprocal267200000.0000
Solution quality estimate total_estimate0.8607
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.0
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.735
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha18900000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.421

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3v7dA00
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_id3v7dB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily50
Domain ID domain_id3v7dB02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id3v7dC00
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_id3v7dD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily50
Domain ID domain_id3v7dD02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)