Research workbench
Crystal structure of the noncanonical ketosynthase faby from P. aeruginosa
Analyse Crystal structure of the noncanonical ketosynthase faby from P. aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CW4
- Type
- protein
- Length
- 639 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-ketoacyl synthase
- UniProt
- Q9HU15
- Ligands
- SO4, CL
- Pockets
- 8 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-ketoacyl synthase | protein | 639 | 39% helix, 21% strand | Q9HU15 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.64 | 0.84 | 30 | empty |
| 2 | 149 | 0.53 | 0.80 | 22 | empty |
| 3 | 59 | 0.53 | 0.87 | 24 | empty |
| 4 | 173 | 0.44 | 0.74 | 27 | empty |
| 5 | 106 | 0.44 | 0.78 | 17 | empty |
Compared structures
- 4CW4 · Crystal structure of the noncanonical ketosynthase FabY from P. aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HU15 · AlphaFold monomer V2.0 prediction for beta-ketoacyl-[acyl-carrier- protein] synthase faby… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9HU15
- Elsewhere: RCSB PDB 4CW4 · PDBe 4CW4 · UniProt Q9HU15
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