Research workbench
Inha (T2A mutant) complexed with 2,6-dimethyl-3-phenylpyridin-4(1H)- one
Analyse Inha (T2A mutant) complexed with 2,6-dimethyl-3-phenylpyridin-4(1H)- one in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OIQ
- Type
- protein
- Length
- 1,020 residues
- Chains
- 4
- 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
- P9WGR1
- Ligands
- 9WB, NAD
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 261 | 44% helix, 17% strand | P9WGR1 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 250 | 45% helix, 18% strand | P9WGR1 |
| C | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 247 | 43% helix, 18% strand | P9WGR1 |
| D | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 262 | 45% helix, 17% strand | P9WGR1 |
Ligands and binding sites
- 9WB · 2,6-dimethyl-3-phenyl-1~{H}-pyridin-4-one · ligand · 4 copies · chains A, B, C, D
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1157 | 0.83 | 0.84 | 53 | empty |
| 2 | 716 | 0.77 | 0.82 | 52 | 9WB, NAD |
| 3 | 782 | 0.77 | 0.80 | 49 | 9WB, NAD |
| 4 | 533 | 0.69 | 0.79 | 44 | 9WB, NAD |
| 5 | 595 | 0.69 | 0.78 | 46 | 9WB, NAD |
Interfaces
6 interfaces between chains.
- A–C · 1556 Ų buried · 21 hydrogen bonds · protein-protein
- B–D · 1553 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 1468 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 1465 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 672 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 5OIQ · InhA (T2A mutant) complexed with 2,6-dimethyl-3-phenylpyridin-4(1H)-one · the same entry in another collection · chain D against D, TM-score 1.00
- P9WGR1 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P9WGR1
- Elsewhere: RCSB PDB 5OIQ · PDBe 5OIQ · UniProt P9WGR1
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