2ovp

Structure of the Skp1-Fbw7 complex

Method: X-RAY DIFFRACTION Dmax: 99.0 Å Quality: GOOD

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

S-phase kinase-associated protein 1A

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–163 Fragment:residues 1-147 F-box/WD repeat protein 7 × 1 (Q969H0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;0.1 M HEPES-Na, 1.2 M Li2SO4, 7.5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.90 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–163 Fragment:residues 1-147 F-box/WD repeat protein 7 × 4 (Q969H0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;0.1 M HEPES-Na, 1.2 M Li2SO4, 7.5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.90 Å R-free 0.268

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 1–135; UniProt 1–163

F-box/WD repeat protein 7

Homo sapiens

UniProt Q969H0

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 263–707 Fragment:N-terminal residues 263-707 S-phase kinase-associated protein 1A × 1 (P63208) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;0.1 M HEPES-Na, 1.2 M Li2SO4, 7.5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.90 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 263–707 Fragment:N-terminal residues 263-707 S-phase kinase-associated protein 1A × 4 (P63208) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;0.1 M HEPES-Na, 1.2 M Li2SO4, 7.5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.90 Å R-free 0.268

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.

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

View Construct and Data Evidence
UniProt name FBXW7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 263–707

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 2ovp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ovp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ovp
Deposition date deposition_date2007-02-14
Structure title titleStructure of the Skp1-Fbw7 complex
Keywords keywordsF-box; WD40 domains, TRANSCRIPTION-CELL CYCLE COMPLEX; TRANSCRIPTION/CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.23
Radius of gyration Rg (electron density) rg_electron29.95
Forward intensity I(0) i068422400.00
Molecular weight molecular_weight64880.0 kDa
Excluded volume excluded_volume81107 ų
Envelope volume envelope_volume96710 ų
Hydration-shell volume shell_volume27934 ų
Envelope diameter envelope_diameter99.9
Shell Rg shell_rg35.89
Envelope Rg envelope_rg29.57
Shape Rg shape_rg29.94
Total Rg total_rg30.54
Total atoms total_atoms4557
Residues n_residues575
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 dmax99.0
Rg (real space) rg_real30.37
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real6.8420e+07
I(0) uncertainty (real space) i0_real_error1.1830e+06
Rg (reciprocal space) rg_reciprocal30.31
I(0) (reciprocal space) i0_reciprocal68420000.0000
Solution quality estimate total_estimate0.8647
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.680
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6617000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.894

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2ovpa1
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_idd2ovpa2
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_idd2ovpb1
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_idd2ovpb2
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 (3 domains)

Domain ID domain_id2ovpA00
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_id2ovpB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily50
Domain ID domain_id2ovpB02
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)