Research workbench
Crystal structure and function of the isoniazid target of mycobacterium tuberculosis
Analyse Crystal structure and function of the isoniazid target of mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ENZ
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-acyl carrier protein (acp) reductase
- UniProt
- P0A5Y6
- Ligands
- NAD
- Pockets
- 2 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-acyl carrier protein (acp) reductase | protein | 268 | 44% helix, 15% strand | P0A5Y6 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 665 | 0.80 | 0.84 | 49 | NAD |
| 2 | 79 | 0.41 | 0.79 | 18 | empty |
Compared structures
- 1ENZ · Crystal structure and function of the isoniazid target of mycobacterium tuberculosis · 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 1ENZ · PDBe 1ENZ · UniProt P0A5Y6
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