1ldk

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex

Method: X-RAY DIFFRACTION Dmax: 158.9 Å Quality: REASONABLE

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

CULLIN HOMOLOG

Homo sapiens

UniProt Q13616

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 15–410 Chain B; UniProt 411–776 Fragment:RESIDUES 15-410 Fragment:RESIDUES 411-776 ring-box protein 1 × 1 (P62877) CYCLIN A/CDK2-ASSOCIATED PROTEIN P19 × 1 (P63208) SKP2-like protein type gamma × 1 (Q13309) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 15–410 Chain B; UniProt 411–776 Fragment:RESIDUES 15-410 Fragment:RESIDUES 411-776 ring-box protein 1 × 2 (P62877) CYCLIN A/CDK2-ASSOCIATED PROTEIN P19 × 2 (P63208) SKP2-like protein type gamma × 2 (Q13309) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331

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.

47 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL1_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–396; UniProt 15–410 Author chain B; PDBConstruct 1–366; UniProt 411–776

ring-box protein 1

Homo sapiens

UniProt P62877

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 19–108 Not recorded CULLIN HOMOLOG × 1 (Q13616) CULLIN HOMOLOG × 1 (Q13616) CYCLIN A/CDK2-ASSOCIATED PROTEIN P19 × 1 (P63208) SKP2-like protein type gamma × 1 (Q13309) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 19–108 Not recorded CULLIN HOMOLOG × 2 (Q13616) CULLIN HOMOLOG × 2 (Q13616) CYCLIN A/CDK2-ASSOCIATED PROTEIN P19 × 2 (P63208) SKP2-like protein type gamma × 2 (Q13309) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331

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.

99 other PDB entries and 106 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–90; UniProt 19–108

CYCLIN A/CDK2-ASSOCIATED PROTEIN P19

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–139 Not recorded CULLIN HOMOLOG × 1 (Q13616) CULLIN HOMOLOG × 1 (Q13616) ring-box protein 1 × 1 (P62877) SKP2-like protein type gamma × 1 (Q13309) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 1–139 Not recorded CULLIN HOMOLOG × 2 (Q13616) CULLIN HOMOLOG × 2 (Q13616) ring-box protein 1 × 2 (P62877) SKP2-like protein type gamma × 2 (Q13309) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331

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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–133; UniProt 1–139

SKP2-like protein type gamma

Homo sapiens

UniProt Q13309

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 97–137 Not recorded CULLIN HOMOLOG × 1 (Q13616) CULLIN HOMOLOG × 1 (Q13616) ring-box protein 1 × 1 (P62877) CYCLIN A/CDK2-ASSOCIATED PROTEIN P19 × 1 (P63208) ZN ZINC ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 97–137 Not recorded CULLIN HOMOLOG × 2 (Q13616) CULLIN HOMOLOG × 2 (Q13616) ring-box protein 1 × 2 (P62877) CYCLIN A/CDK2-ASSOCIATED PROTEIN P19 × 2 (P63208) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;peg4k, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 3.10 Å R-free 0.331

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.

25 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–41; UniProt 97–137

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 1ldk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ldk
Deposition date deposition_date2002-04-08
Structure title titleStructure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex
Keywords keywordsSCF, cullin, rbx1, roc1, hrt1, skp1, skp2, F-box, fbox, ubiquitin, ubiquitination, E3 ligase, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier52.49
Radius of gyration Rg (electron density) rg_electron53.18
Forward intensity I(0) i0181389000.00
Molecular weight molecular_weight112880.0 kDa
Excluded volume excluded_volume141900 ų
Envelope volume envelope_volume235950 ų
Hydration-shell volume shell_volume38931 ų
Envelope diameter envelope_diameter168.3
Shell Rg shell_rg52.84
Envelope Rg envelope_rg50.64
Shape Rg shape_rg53.18
Total Rg total_rg53.15
Total atoms total_atoms7922
Residues n_residues971
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 dmax158.9
Rg (real space) rg_real52.94
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real1.8140e+08
I(0) uncertainty (real space) i0_real_error3.6990e+06
Rg (reciprocal space) rg_reciprocal52.08
I(0) (reciprocal space) i0_reciprocal181200000.0000
Solution quality estimate total_estimate0.7057
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-1.022
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7030000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.580; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.429; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1ldka_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.17 — Cullin repeat-like
Family Family familya.118.17.1 — Cullin repeat
Domain ID domain_idd1ldkb1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.34 — SCF ubiquitin ligase complex WHB domain
Domain ID domain_idd1ldkb2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.40 — Cullin homology domain
Superfamily Superfamily superfamilye.40.1 — Cullin homology domain
Family Family familye.40.1.1 — Cullin homology domain
Domain ID domain_idd1ldkc_
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4
Domain ID domain_idd1ldkd1
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_idd1ldkd2
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_idd1ldke1
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

CATH v4.4 (9 domains)

Domain ID domain_id1ldkA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id1ldkA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id1ldkA03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id1ldkB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1310 — 5 helical Cullin repeat like
Homologous superfamily homologous superfamily10 — Cullin Repeats
Domain ID domain_id1ldkB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology230 — Ribosomal Protein S5; domain 2
Homologous superfamily homologous superfamily130 — Cullin; Chain C, Domain 2
Domain ID domain_id1ldkB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id1ldkC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id1ldkD00
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_id1ldkE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1280 — Monooxygenase
Homologous superfamily homologous superfamily50

8. Citations (1)

9. Files and Curves (10)