Research workbench
AlphaFold monomer V2.0 prediction for formate hydrogenlyase subunit 7 (P16433)
Analyse AlphaFold monomer V2.0 prediction for formate hydrogenlyase subunit 7 (P16433) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P16433
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB74A3a10Bdfe3C1226B2CF28959A9C5F69dc531D
- UniProt
- P16433
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 255 | — | P16433 |
Compared structures
- 7Z0T · Structure of the Escherichia coli formate hydrogenlyase complex (aerobic preparation… · an experimental structure of the same protein · chain A against G, TM-score 0.49
- 7Z0S · Structure of the Escherichia coli formate hydrogenlyase complex (anaerobic preparation… · an experimental structure of the same protein · chain A against G, TM-score 0.49
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 P16433
- Elsewhere: UniProt P16433 · AlphaFold DB P16433
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