MolNFT v1 · #225750 · protein
AlphaFold monomer V2.0 prediction for hydrogenase-1 large chain (P0ACD8)
P0ACD8: “AlphaFold monomer V2.0 prediction for hydrogenase-1 large chain (P0ACD8)”. MolNFT v1 #225750 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P0ACD8
- Type
- protein
- Length
- 597 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x091554B316044d26D7307E7F5d45AEFbD0138EB3
- UniProt
- P0ACD8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 597 | — | P0ACD8 |
Compared structures
- 6RP2 · Threonine to Cysteine (T225C) variant of E coli hydrogenase-1 · an experimental structure of the same protein · chain A against M, TM-score 0.97
- 5A4I · The mechanism of Hydrogen activation by NiFE-hydrogenases · an experimental structure of the same protein · chain A against M, TM-score 0.97
- 6G7R · Structure of fully reduced variant E28Q of E. coli hydrogenase-1 at pH 8 · an experimental structure of the same protein · chain A against M, TM-score 0.97
- 6G94 · Structure of E. coli hydrogenase-1 C19G variant in complex with cytochrome b · an experimental structure of the same protein · chain A against J, TM-score 0.97
- 5A4M · Mechanism of hydrogen activation by nife-hydrogenases · an experimental structure of the same protein · chain A against L, TM-score 0.97
- 4UE3 · The Mechanism of Hydrogen Activation by NiFe-hydrogenases and the Importance of the… · an experimental structure of the same protein · chain A against LLL, TM-score 0.97
- 6GAL · Structure of fully reduced Hydrogenase (Hyd-1) variant E28Q collected at pH 10 · an experimental structure of the same protein · chain A against M, TM-score 0.97
- 5A4I · The mechanism of hydrogen activation by nife-hydrogenases · an experimental structure of the same protein · chain A against L, TM-score 0.97
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 P0ACD8
- Elsewhere: UniProt P0ACD8 · AlphaFold DB P0ACD8
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