Research workbench
The structure of monooxygenase KSTA11 in the biosynthetic pathway of kosinostatin
Analyse The structure of monooxygenase KSTA11 in the biosynthetic pathway of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F5L
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monooxygenase
- UniProt
- A0A023GUL3
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Monooxygenase | protein | 290 | 44% helix, 19% strand | A0A023GUL3 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 474 | 0.70 | 0.80 | 65 | GOL |
| 2 | 63 | 0.35 | 0.77 | 14 | GOL |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 5F5L · The structure of monooxygenase KstA11 in the biosynthetic pathway of kosinostatin · 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 A0A023GUL3
- Elsewhere: RCSB PDB 5F5L · PDBe 5F5L · UniProt A0A023GUL3
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