MolNFT v2 · #172543 · protein
[Fe]-hydrogenase from Methanolacinia paynteri with bound guanylylpyridinol at 1.7-A resolution
6YK9: “[Fe]-hydrogenase from Methanolacinia paynteri with bound guanylylpyridinol at 1.7-A resolution”. X-ray diffraction at 1.7, 3 ligands (5GP, FEG, GMP). MolNFT v2 #172543 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YK9
- Type
- protein
- Length
- 1,366 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.7
- Source
- Methanolacinia paynteri G-2000
- Ligands
- 5GP, FEG, GMP
Structure
x-ray diffraction · resolution 1.7 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 342 | — | — |
| C, E | — | protein | 341 | — | — |
Ligands and binding sites
- 5GP · Guanosine-5'-monophosphate · ligand · 2 copies · chains B, C
- FEG · 5'-O-[(S)-{[2-(carboxymethyl)-6-hydroxy-3,5-dimethylpyridin-4-yl]oxy}(hydroxy)phosphoryl]guanosine · ligand · chains A
- GMP · Guanosine · ligand · chains E
- EDO · 1,2-ethanediol · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YK9 · [fe]-hydrogenase from methanolacinia paynteri with bound guanylylpyridinol at 1.7-a… · 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
- Elsewhere: RCSB PDB 6YK9 · PDBe 6YK9
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