Research workbench
The effect of isoleucine to alanine mutation on inha enzyme crystallization pattern and inhibition by ligand PT70 (tcu)
Analyse The effect of isoleucine to alanine mutation on inha enzyme crystallization… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CPB
- Type
- protein
- Length
- 1,575 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
- M9TGV3
- Ligands
- NAD
- Pockets
- 18 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 268 | 47% helix, 16% strand | M9TGV3 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 246 | 43% helix, 18% strand | M9TGV3 |
| E | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 260 | 45% helix, 17% strand | M9TGV3 |
| F | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 265 | 44% helix, 17% strand | M9TGV3 |
Ligands and binding sites
- 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
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1136 | 0.83 | 0.85 | 57 | empty |
| 2 | 952 | 0.80 | 0.82 | 74 | NAD |
| 3 | 881 | 0.79 | 0.82 | 64 | NAD |
| 4 | 981 | 0.79 | 0.81 | 72 | NAD |
| 5 | 690 | 0.78 | 0.82 | 63 | NAD |
Interfaces
9 interfaces between chains.
- E–F · 1559 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 1549 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 1508 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 1487 Ų buried · 19 hydrogen bonds · protein-protein
- B–F · 1449 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 5CPB · The effect of isoleucine to alanine mutation on InhA enzyme crystallization pattern and… · 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 M9TGV3
- Elsewhere: RCSB PDB 5CPB · PDBe 5CPB · UniProt M9TGV3
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