MolNFT v2 · #172751 · protein
Promiscuous Reductase LugOII Catalyzes Keto-reduction at C1 during Lugdunomycin Biosynthesis
6YQ6: “Promiscuous Reductase LugOII Catalyzes Keto-reduction at C1 during Lugdunomycin Biosynthesis”. X-ray diffraction at 2.08, 1 ligand (SO4). MolNFT v2 #172751 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YQ6
- Type
- protein
- Length
- 475 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.08
- Source
- Streptomyces sp. QL37
- UniProt
- A0A2S6PN47
- Ligands
- SO4
Structure
x-ray diffraction · resolution 2.08 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| AAA | — | protein | 231 | — | A0A2S6PN47 |
| BBB | — | protein | 244 | — | A0A2S6PN47 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains AAA, BBB
- EDO · 1,2-ethanediol · additive · 16 copies · chains AAA, BBB
- PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains AAA, BBB
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 A0A2S6PN47
- Elsewhere: RCSB PDB 6YQ6 · PDBe 6YQ6 · UniProt A0A2S6PN47
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