Research workbench
AlphaFold monomer V2.0 prediction for 4-hydroxybutyrate--CoA ligase 1 (A4YDT1)
Analyse AlphaFold monomer V2.0 prediction for 4-hydroxybutyrate--CoA ligase 1 (A4YDT1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4YDT1
- Type
- protein
- Length
- 564 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- UniProt
- A4YDT1
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 564 | — | A4YDT1 |
Compared structures
- 8BIQ · Crystal structure of acyl-COA synthetase from Metallosphaera sedula in complex with… · an experimental structure of the same protein · chain A against A, TM-score 0.82
- 8BIT · Crystal structure of acyl-CoA synthetase from Metallosphaera sedula in complex with… · an experimental structure of the same protein · chain A against B, TM-score 0.81
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 A4YDT1
- Elsewhere: UniProt A4YDT1 · AlphaFold DB A4YDT1
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