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The crystal structure of [fe]-hydrogenase (hmd) holoenzyme from methanocaldococcus jannaschii
Analyse The crystal structure of [fe]-hydrogenase (hmd) holoenzyme from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F47
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q58194
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 344 | — | Q58194 |
Compared structures
- 3F47 · The Crystal Structure of [Fe]-Hydrogenase (Hmd) Holoenzyme from Methanocaldococcus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q58194 · AlphaFold monomer V2.0 prediction for 5,10-methenyltetrahydromethanopterin hydrogenase… · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q58194
- Elsewhere: RCSB PDB 3F47 · PDBe 3F47 · UniProt Q58194
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