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The first ketoreductase of the tylosin PKS
Analyse The first ketoreductase of the tylosin PKS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z5L
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Streptomyces fradiae
- Molecule
- Tylactone synthase starter module and modules 1 & 2
- EC
- 1.1.1.100
- UniProt
- O33954
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tylactone synthase starter module and modules 1 & 2 (EC 1.1.1.100) | protein | 453 | 43% helix, 20% strand | O33954 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.75 | 0.96 | 29 | empty |
| 2 | 311 | 0.68 | 0.83 | 40 | empty |
| 3 | 200 | 0.68 | 0.86 | 30 | empty |
| 4 | 77 | 0.51 | 0.85 | 16 | empty |
Compared structures
- 2Z5L · The first ketoreductase of the tylosin pks · 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 O33954
- Elsewhere: RCSB PDB 2Z5L · PDBe 2Z5L · UniProt O33954
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