Research workbench
AlphaFold monomer V2.0 prediction for probable NI/FE-hydrogenase 1 B-type cytochrome subunit (P0AAM1)
Analyse AlphaFold monomer V2.0 prediction for probable NI/FE-hydrogenase 1 B-type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AAM1
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- UniProt
- P0AAM1
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 235 | — | P0AAM1 |
Compared structures
- 4GD3 · Structure of E. coli hydrogenase-1 in complex with cytochrome b · an experimental structure of the same protein · chain A against A, TM-score 0.66
- 4GD3 · Structure of E. COLI hydrogenase-1 in complex with cytochrome B · an experimental structure of the same protein · chain A against A, TM-score 0.66
- 6G94 · Structure of E. COLI hydrogenase-1 C19G variant in complex with cytochrome B · an experimental structure of the same protein · chain A against A, TM-score 0.66
- 6G94 · Structure of E. coli hydrogenase-1 C19G variant in complex with cytochrome b · an experimental structure of the same protein · chain A against A, TM-score 0.66
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 P0AAM1
- Elsewhere: UniProt P0AAM1 · AlphaFold DB P0AAM1
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