MolNFT v1 · #19715 · protein
Crystal structure of enoyl reductase inhibition by triclosan
1QSG · Enoyl-[acyl-carrier-protein] reductase: “Crystal structure of enoyl reductase inhibition by triclosan”. X-ray diffraction, 3 ligands (NAD, TCL, GLC), 20 pockets (best druggability 0.84). MolNFT v1 #19715 on GenesisL1: 3D structure…
- PDB
- 1QSG
- Type
- protein
- Length
- 2,065 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase
- EC
- 1.3.1.9
- UniProt
- P29132
- Ligands
- NAD, TCL, GLC
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, H | Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.9) | protein | 258 | 47% helix, 17% strand | P29132 |
| G | Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.9) | protein | 259 | 49% helix, 17% strand | P29132 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- TCL · Triclosan · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1103 | 0.84 | 0.85 | 52 | empty |
| 2 | 1126 | 0.83 | 0.85 | 52 | empty |
| 3 | 720 | 0.81 | 0.85 | 56 | GLC, NAD, TCL |
| 4 | 504 | 0.80 | 0.87 | 48 | GLC, NAD, TCL |
| 5 | 544 | 0.80 | 0.86 | 43 | NAD, TCL |
Interfaces
14 interfaces between chains.
- A–B · 1742 Ų buried · 40 hydrogen bonds · protein-protein
- G–H · 1740 Ų buried · 40 hydrogen bonds · protein-protein
- E–F · 1739 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 1738 Ų buried · 40 hydrogen bonds · protein-protein
- B–D · 1384 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1QSG · Crystal structure of enoyl reductase inhibition by triclosan · 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 P29132
- Elsewhere: RCSB PDB 1QSG · PDBe 1QSG · UniProt P29132
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