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Crystal structure of [fe]-hydrogenase (hmd) holoenzyme from methanococcus aeolicus (open form)
Analyse Crystal structure of [fe]-hydrogenase (hmd) holoenzyme from methanococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HAC
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A6UVT1
- Ligands
- FE9, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 342 | — | A6UVT1 |
Ligands and binding sites
- FE9 · iron-guanylyl pyridinol cofactor · ligand · chains A
- NA · Sodium ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HAC · Crystal structure of [Fe]-hydrogenase (Hmd) holoenzyme from Methanococcus aeolicus (open… · 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 A6UVT1
- Elsewhere: RCSB PDB 6HAC · PDBe 6HAC · UniProt A6UVT1
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