Research workbench
3D structure of the ni-fe-se hydrogenase from D. vulgaris hildenborough in the reduced state at 1.95 ångströms
Analyse 3D structure of the ni-fe-se hydrogenase from D. vulgaris hildenborough in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZE7
- Type
- protein
- Length
- 758 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q72AS4, Q72AS3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 277 | — | Q72AS4 |
| B | — | protein | 481 | — | Q72AS3 |
Compared structures
- 3ZE7 · 3D structure of the Ni-Fe-Se hydrogenase from D. vulgaris Hildenborough in the reduced… · the same entry in another collection · chain A 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 Q72AS4
- Every structure of UniProt Q72AS3
- Elsewhere: RCSB PDB 3ZE7 · PDBe 3ZE7 · UniProt Q72AS4 · UniProt Q72AS3
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