Research workbench
Crystal structure of mycobacterium tuberculosis enoyl reductase (inha) inhibited by 5-pentyl-2-phenoxyphenol
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
- 2B36
- Type
- protein
- Length
- 1,528 residues
- Chains
- 6
- 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
- P0A5Y6
- Ligands
- 5PP, NAD
- Pockets
- 15 · best druggability 0.83
Structure
x-ray diffraction · 6 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 268 | 42% helix, 16% strand | P0A5Y6 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 259 | 46% 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 | 43% helix, 18% strand | P0A5Y6 |
| E | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 254 | 45% helix, 17% strand | P0A5Y6 |
| F | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 251 | 43% helix, 18% strand | P0A5Y6 |
Ligands and binding sites
- 5PP · 5-pentyl-2-phenoxyphenol · 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
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1118 | 0.83 | 0.85 | 60 | empty |
| 2 | 902 | 0.80 | 0.82 | 87 | 5PP, NAD |
| 3 | 835 | 0.79 | 0.82 | 69 | 5PP, NAD |
| 4 | 1115 | 0.77 | 0.79 | 105 | empty |
| 5 | 642 | 0.72 | 0.79 | 48 | 5PP, NAD |
Interfaces
9 interfaces between chains.
- E–F · 1553 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1545 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1536 Ų buried · 25 hydrogen bonds · protein-protein
- C–F · 1489 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1487 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 2B36 · 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 2B36 · PDBe 2B36 · UniProt P0A5Y6
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