Research workbench
Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (fabg) from pseudomonas aeruginosa in complex with 2-phenyl-4-(1,2,4- triazol-4-YL)QUINAZOLINE at 2.0A resolution
Analyse Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (fabg) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BNU
- Type
- protein
- Length
- 976 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
- O54438
- Ligands
- 9KQ
- Pockets
- 11 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 239 | 49% helix, 16% strand | O54438 |
| B | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 240 | 50% helix, 16% strand | O54438 |
| C | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 251 | 48% helix, 17% strand | O54438 |
| D | 3-oxoacyl-[acyl-carrier-protein] reductase fabg (EC 1.1.1.100) | protein | 246 | 49% helix, 16% strand | O54438 |
Ligands and binding sites
- 9KQ · 2-phenyl-4-(1,2,4-triazol-4-yl)quinazoline · ligand · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1147 | 0.82 | 0.83 | 86 | empty |
| 2 | 140 | 0.78 | 0.95 | 24 | 9KQ |
| 3 | 142 | 0.76 | 0.93 | 24 | 9KQ |
| 4 | 868 | 0.75 | 0.79 | 86 | empty |
| 5 | 441 | 0.66 | 0.79 | 46 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1728 Ų buried · 22 hydrogen bonds · protein-protein
- A–D · 1522 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 915 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 897 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 279 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4BNU · Crystal structure of 3-oxoacyl-(acyl-carrier-protein) reductase (FabG) from Pseudomonas… · the same entry in another collection · chain D against D, TM-score 1.00
- O54438 · 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 0.92
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 O54438
- Elsewhere: RCSB PDB 4BNU · PDBe 4BNU · UniProt O54438
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.