Research workbench
WD40 domain of arabidopsis thaliana E3 ubiquitin ligase COP1 in complex with peptide from TRIB1
Analyse WD40 domain of arabidopsis thaliana E3 ubiquitin ligase COP1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.