Research workbench
The mechanism of hydrogen activation by nife-hydrogenases
Analyse The mechanism of hydrogen activation by nife-hydrogenases in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A4I
- Type
- protein
- Length
- 1,690 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ACD8, P69739
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, M | — | protein | 581 | — | P0ACD8 |
| S, T | — | protein | 264 | — | P69739 |
Compared structures
- 5A4I · The mechanism of Hydrogen activation by NiFE-hydrogenases · the same entry in another collection · chain L against L, TM-score 1.00
- P0ACD8 · AlphaFold monomer V2.0 prediction for hydrogenase-1 large chain (P0ACD8) · a predicted model of the same protein · chain L against A, TM-score 1.00
- P69739 · AlphaFold monomer V2.0 prediction for hydrogenase-1 small chain (P69739) · a predicted model of the same protein · chain S against A, TM-score 1.00
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
- Every structure of UniProt P69739
- Elsewhere: RCSB PDB 5A4I · PDBe 5A4I · UniProt P0ACD8 · UniProt P69739
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