Research workbench
Crystal structures of fabi from F. tularensis in complex with novel inhibitors based on the benzimidazole scaffold
Analyse Crystal structures of fabi from F. tularensis in complex with novel inhibitors… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J1N
- Type
- protein
- Length
- 516 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase [NADH]
- EC
- 1.3.1.9
- UniProt
- Q5NGQ3
- Ligands
- NAD, 1JN
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 258 | 50% helix, 14% strand | Q5NGQ3 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- 1JN · 1-(4-methoxy-3-methylbenzyl)-1,5,6,7-tetrahydroindeno[5,6-d]imidazole · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
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 | 585 | 0.79 | 0.85 | 48 | NAD, 1JN |
| 2 | 581 | 0.79 | 0.84 | 52 | NAD, 1JN |
| 3 | 186 | 0.42 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1374 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4J1N · Crystal structures of FabI from F. tularensis in complex with novel inhibitors based on… · the same entry in another collection · chain A 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 Q5NGQ3
- Elsewhere: RCSB PDB 4J1N · PDBe 4J1N · UniProt Q5NGQ3
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