Research workbench
AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (B1X6V8)
Analyse AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1X6V8
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaf4ABF15a4d74bcB5a3C972147FC3C36D9b5083E
- UniProt
- B1X6V8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 356 | — | B1X6V8 |
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 B1X6V8
- Elsewhere: UniProt B1X6V8 · AlphaFold DB B1X6V8
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