1nex

Crystal Structure of ScSkp1-ScCdc4-CPD peptide complex

Method: X-RAY DIFFRACTION Dmax: 139.7 Å Quality: GOOD

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

Centromere DNA-binding protein complex CBF3 subunit D

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 1–193 Fragment:residues 36-63 deleted Non-standard monomer:Yes (specific site not provided by mmCIF) CDC4 protein × 1 (P07834) GLL(TPO)PPQSG × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;Ammonium Sulphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.273
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–193 Fragment:residues 36-63 deleted Non-standard monomer:Yes (specific site not provided by mmCIF) CDC4 protein × 1 (P07834) GLL(TPO)PPQSG × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;Ammonium Sulphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.273

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 1–193 Author chain C; PDBConstruct 4–169; UniProt 1–193

CDC4 protein

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:residues 601-604 and 609-624 deleted Mutation:C608L Non-standard monomer:Yes (specific site not provided by mmCIF) Centromere DNA-binding protein complex CBF3 subunit D × 1 (P52286) GLL(TPO)PPQSG × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;Ammonium Sulphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.273
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 263–744 Fragment:residues 601-604 and 609-624 deleted Mutation:C608L Non-standard monomer:Yes (specific site not provided by mmCIF) Centromere DNA-binding protein complex CBF3 subunit D × 1 (P52286) GLL(TPO)PPQSG × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;Ammonium Sulphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.273

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

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 1nex

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1nex
Deposition date deposition_date2002-12-12
Structure title titleCrystal Structure of ScSkp1-ScCdc4-CPD peptide complex
Keywords keywordsWD 40 domain, phospho-peptide complex, E3 ubiquitin ligase, LIGASE, CELL CYCLE; LIGASE, CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.35
Radius of gyration Rg (electron density) rg_electron43.95
Forward intensity I(0) i0259410000.00
Molecular weight molecular_weight133590.0 kDa
Excluded volume excluded_volume167640 ų
Envelope volume envelope_volume238070 ų
Hydration-shell volume shell_volume46794 ų
Envelope diameter envelope_diameter138.0
Shell Rg shell_rg47.19
Envelope Rg envelope_rg42.29
Shape Rg shape_rg43.91
Total Rg total_rg44.24
Total atoms total_atoms9363
Residues n_residues1139
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 dmax139.7
Rg (real space) rg_real44.45
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real2.5940e+08
I(0) uncertainty (real space) i0_real_error4.5390e+06
Rg (reciprocal space) rg_reciprocal44.35
I(0) (reciprocal space) i0_reciprocal259400000.0000
Solution quality estimate total_estimate0.8302
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.8
Skewness Skewness skewness0.233
Kurtosis Kurtosis kurtosis-0.761
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16830000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1nexa1
Class classa — All alpha proteins
Fold Fold folda.157 — Skp1 dimerisation domain-like
Superfamily Superfamily superfamilya.157.1 — Skp1 dimerisation domain-like
Family Family familya.157.1.1 — Skp1 dimerisation domain-like
Domain ID domain_idd1nexa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.1 — BTB/POZ domain
Domain ID domain_idd1nexb1
Class classa — All alpha proteins
Fold Fold folda.158 — F-box domain
Superfamily Superfamily superfamilya.158.1 — F-box domain
Family Family familya.158.1.1 — F-box domain
Domain ID domain_idd1nexb2
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.1 — WD40-repeat
Domain ID domain_idd1nexc1
Class classa — All alpha proteins
Fold Fold folda.157 — Skp1 dimerisation domain-like
Superfamily Superfamily superfamilya.157.1 — Skp1 dimerisation domain-like
Family Family familya.157.1.1 — Skp1 dimerisation domain-like
Domain ID domain_idd1nexc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.42 — POZ domain
Superfamily Superfamily superfamilyd.42.1 — POZ domain
Family Family familyd.42.1.1 — BTB/POZ domain
Domain ID domain_idd1nexd1
Class classa — All alpha proteins
Fold Fold folda.158 — F-box domain
Superfamily Superfamily superfamilya.158.1 — F-box domain
Family Family familya.158.1.1 — F-box domain
Domain ID domain_idd1nexd2
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.1 — WD40-repeat

CATH v4.4 (6 domains)

Domain ID domain_id1nexA00
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_id1nexB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily50
Domain ID domain_id1nexB02
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_id1nexC00
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_id1nexD01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily50
Domain ID domain_id1nexD02
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)