Research workbench
AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (B2FPM0)
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
- B2FPM0
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcB690B5E3a35d70EE98529ec0d65d824111EE793
- UniProt
- B2FPM0
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 364 | — | B2FPM0 |
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 B2FPM0
- Elsewhere: UniProt B2FPM0 · AlphaFold DB B2FPM0
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