Research workbench
Mups, a 3-oxoacyl (acp) reductase involved in mupirocin biosynthesis
Analyse Mups, a 3-oxoacyl (acp) reductase involved in mupirocin biosynthesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YXF
- Type
- protein
- Length
- 457 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mups
- UniProt
- Q8RL53
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mups | protein | 230 | 47% helix, 18% strand | Q8RL53 |
| B | Mups | protein | 227 | 45% helix, 17% strand | Q8RL53 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.55 | 0.75 | 36 | empty |
| 2 | 267 | 0.52 | 0.75 | 35 | empty |
| 3 | 85 | 0.38 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1587 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 4YXF · MupS, a 3-oxoacyl (ACP) reductase involved in Mupirocin biosynthesis · 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 Q8RL53
- Elsewhere: RCSB PDB 4YXF · PDBe 4YXF · UniProt Q8RL53
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