Research workbench
Crystal structure of S. aureus fabh, beta-ketoacyl carrier protein synthase III
Analyse Crystal structure of S. aureus fabh, beta-ketoacyl carrier protein synthase III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZOW
- Type
- protein
- Length
- 1,248 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] synthase III
- EC
- 2.3.1.41
- UniProt
- Q8NXE2
- Pockets
- 11 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 3-oxoacyl-[acyl-carrier-protein] synthase III (EC 2.3.1.41) | protein | 312 | 41% helix, 26% strand | Q8NXE2 |
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.69 | 0.88 | 32 | empty |
| 2 | 452 | 0.69 | 0.80 | 34 | empty |
| 3 | 460 | 0.68 | 0.79 | 36 | empty |
| 4 | 169 | 0.67 | 0.86 | 34 | empty |
| 5 | 170 | 0.67 | 0.86 | 39 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2051 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 2018 Ų buried · 30 hydrogen bonds · protein-protein
- A–C · 732 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1ZOW · Crystal Structure of S. aureus FabH, beta-ketoacyl carrier protein synthase III · the same entry in another collection · chain C against C, TM-score 1.00
- Q8NXE2 · AlphaFold monomer V2.0 prediction for 3-oxoacyl-[acyl-carrier- protein] synthase 3… · a predicted model of the same protein · chain D 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 Q8NXE2
- Elsewhere: RCSB PDB 1ZOW · PDBe 1ZOW · UniProt Q8NXE2
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