5igo

WD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from Trib1

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

E3 ubiquitin-protein ligase COP1

Arabidopsis thaliana

UniProt P43254

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Tribbles homolog 1 × 1 (Q96RU8) water × 2 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 Tribbles homolog 1 × 1 (Q96RU8) water × 2 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 2 Tribbles homolog 1 × 1 (Q96RU8) water × 2 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 2 Tribbles homolog 1 × 1 (Q96RU8) water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name COP1_ARATH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–336; UniProt 349–675 Author chain B; PDBConstruct 10–336; UniProt 349–675 Author chain C; PDBConstruct 10–336; UniProt 349–675 Author chain D; PDBConstruct 10–336; UniProt 349–675

Tribbles homolog 1

OrganismNot specified

UniProt Q96RU8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 E3 ubiquitin-protein ligase COP1 × 1 (P43254) water × 2 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 E3 ubiquitin-protein ligase COP1 × 1 (P43254) water × 2 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 2 E3 ubiquitin-protein ligase COP1 × 1 (P43254) water × 2 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 2 E3 ubiquitin-protein ligase COP1 × 1 (P43254) water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name TRIB1_HUMAN
Isoform Q96RU8-2
PDB entities 2
Chains and sequence ranges Author chain U; PDBConstruct 1–8; UniProt 188–195 Author chain V; PDBConstruct 1–8; UniProt 188–195 Author chain W; PDBConstruct 1–8; UniProt 188–195 Author chain X; PDBConstruct 1–8; UniProt 188–195

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id5igo
Deposition date deposition_date2016-02-28
Structure title titleWD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from Trib1
Keywords keywordsWD40 domain E3 ligase, Hydrolase-Peptide Complex; Hydrolase/Peptide
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5igo__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5igo__assembly_3__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5igo__assembly_3__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)19.77 Å
Rg (electron density)18.57 Å
Total Rg19.51 Å
Atom count2579
Residues331
Excluded volume45394 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5igo__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 5igo__assembly_2__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 5igo__assembly_3__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 5igo__assembly_4__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5igoA00
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_id5igoB00
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_id5igoC00
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_id5igoD00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
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7. Citations (1)