MolNFT v1 · #122151 · protein
WD40 domain of arabidopsis thaliana E3 ubiquitin ligase COP1 in complex with peptide from TRIB1
5IGO: “WD40 domain of arabidopsis thaliana E3 ubiquitin ligase COP1 in complex with peptide from TRIB1”. X-ray diffraction. MolNFT v1 #122151 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5IGO
- Type
- protein
- Length
- 1,319 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P43254, Q96RU8
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 321 | — | P43254 |
| U, V, W, X | — | protein | 8 | — | Q96RU8 |
| B | — | protein | 321 | — | P43254 |
| C | — | protein | 323 | — | P43254 |
| D | — | protein | 322 | — | P43254 |
Compared structures
- 5IGO · WD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from… · the same entry in another collection · chain W against W, TM-score 1.00
- P43254 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase COP1 (P43254) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P43254
- Every structure of UniProt Q96RU8
- Elsewhere: RCSB PDB 5IGO · PDBe 5IGO · UniProt P43254 · UniProt Q96RU8
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