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Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FABG)(Q152A) from vibrio cholerae
Analyse Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FABG)(Q152A)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5END
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- 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
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 228 | 53% helix, 18% strand | Q9KQH7 |
| B | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 226 | 52% helix, 17% strand | Q9KQH7 |
Ligands and binding sites
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.55 | 0.76 | 44 | empty |
| 2 | 231 | 0.51 | 0.76 | 35 | empty |
| 3 | 81 | 0.47 | 0.82 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1450 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 5END · Crystal structure of beta-ketoacyl-acyl carrier protein reductase (FabG)(Q152A) from… · the same entry in another collection · chain A against A, 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 B against A, TM-score 0.96
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 5END · PDBe 5END · UniProt Q9KQH7
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