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Crystal structure of Mycobacterium tuberculosis enoyl reductase (InhA) inhibited by triclosan
Analyse Crystal structure of Mycobacterium tuberculosis enoyl reductase (InhA)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B35
- Type
- protein
- Length
- 1,500 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Mycobacterium tuberculosis
- Molecule
- Enoyl-[acyl-carrier-protein] reductase [NADH]
- EC
- 1.3.1.9
- UniProt
- P0A5Y6
- Ligands
- TCL, NAD
- Pockets
- 16 · best druggability 0.84
Structure
x-ray diffraction · resolution 2.3 · 6 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 253 | 44% helix, 17% strand | P0A5Y6 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 246 | 43% helix, 17% strand | P0A5Y6 |
| C | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 248 | 44% helix, 18% strand | P0A5Y6 |
| D | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 248 | 42% helix, 18% strand | P0A5Y6 |
| E | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 254 | 44% helix, 17% strand | P0A5Y6 |
| F | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 251 | 43% helix, 16% strand | P0A5Y6 |
Ligands and binding sites
- TCL · Triclosan · ligand · 6 copies · chains A, B, C, D, E, F
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1011 | 0.84 | 0.85 | 53 | empty |
| 2 | 1141 | 0.78 | 0.80 | 131 | empty |
| 3 | 629 | 0.78 | 0.83 | 49 | TCL, NAD |
| 4 | 568 | 0.72 | 0.79 | 44 | TCL, NAD |
| 5 | 558 | 0.69 | 0.78 | 48 | TCL, NAD |
Interfaces
10 interfaces between chains.
- C–D · 1571 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1563 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1563 Ų buried · 19 hydrogen bonds · protein-protein
- C–F · 1502 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1501 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2B35 · Crystal structure of mycobacterium tuberculosis enoyl reductase (inha) inhibited by… · 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 P0A5Y6
- Elsewhere: RCSB PDB 2B35 · PDBe 2B35 · UniProt P0A5Y6
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