Research workbench
AlphaFold monomer V2.0 prediction for hydrogenase 3 maturation protease (P0AEV9)
Analyse AlphaFold monomer V2.0 prediction for hydrogenase 3 maturation protease (P0AEV9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AEV9
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5716E0C0A2EB9DcC8eD670e047355BEe525753dE
- UniProt
- P0AEV9
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 156 | — | P0AEV9 |
Compared structures
- 2E85 · Crystal Structure of the Hydrogenase 3 Maturation protease · an experimental structure of the same protein · chain A against B, TM-score 0.95
- 2E85 · Crystal structure of the hydrogenase 3 maturation protease · an experimental structure of the same protein · chain A against B, TM-score 0.95
- 2I8L · Solution Structure of an endopeptidase HycI from Escherichia coli · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 2I8L · Solution structure of an endopeptidase hyci from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.92
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 P0AEV9
- Elsewhere: UniProt P0AEV9 · AlphaFold DB P0AEV9
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