Research workbench
AlphaFold monomer V2.0 prediction for fosfomycin biosynthesis bifunctional protein FOM1 (P96074)
Analyse AlphaFold monomer V2.0 prediction for fosfomycin biosynthesis bifunctional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P96074
- Type
- protein
- Length
- 435 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- UniProt
- P96074
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 435 | — | P96074 |
Compared structures
- 5X3D · Crystal structure of hep-cmp-bound form of cytidylyltransferase (cytase) domain of FOM1… · an experimental structure of the same protein · chain A against A, TM-score 0.29
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 P96074
- Elsewhere: UniProt P96074 · AlphaFold DB P96074
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