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Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FABG)(G141A) from vibrio cholerae
Analyse Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FABG)(G141A)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WJZ
- Type
- protein
- Length
- 886 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-[acyl-carrier-protein] reductase fabg
- EC
- 1.1.1.100
- UniProt
- Q9KQH7
- Ligands
- PO4
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 224 | 50% helix, 17% strand | Q9KQH7 |
| B | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 218 | 50% helix, 18% strand | Q9KQH7 |
| C | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 225 | 48% helix, 17% strand | Q9KQH7 |
| D | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 219 | 51% helix, 18% strand | Q9KQH7 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1169 | 0.83 | 0.84 | 110 | empty |
| 2 | 375 | 0.65 | 0.79 | 43 | empty |
| 3 | 215 | 0.58 | 0.80 | 33 | empty |
| 4 | 293 | 0.56 | 0.76 | 33 | empty |
| 5 | 246 | 0.54 | 0.77 | 42 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1594 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1586 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 405 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 376 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 56 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4WJZ · Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(G141A) from… · the same entry in another collection · chain D against D, TM-score 1.00
- Q9KQH7 · AlphaFold monomer V2.0 prediction for 3-oxoacyl-[acyl-carrier- protein] reductase fabg… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9KQH7
- Elsewhere: RCSB PDB 4WJZ · PDBe 4WJZ · UniProt Q9KQH7
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