MolNFT v1 · #29752 · protein
Long fatty acid chain enoyl-acp reductase (inha) in complex with an isonicotinic-acyl-NADH inhibitor
1ZID · Enoyl-[acyl-carrier-protein] reductase: “Long fatty acid chain enoyl-acp reductase (inha) in complex with an isonicotinic-acyl-NADH inhibitor”. X-ray diffraction, 1 ligand (ZID), 1 pocket (best druggability 0.81). MolNFT v1 #29752…
- PDB
- 1ZID
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase
- EC
- 1.3.1.9
- UniProt
- P0A5Y6
- Ligands
- ZID
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase (EC 1.3.1.9) | protein | 268 | 47% helix, 16% strand | P0A5Y6 |
Ligands and binding sites
- ZID · Isonicotinic-acetyl-nicotinamide-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 809 | 0.81 | 0.83 | 67 | ZID |
Compared structures
- 1ZID · Long fatty acid chain enoyl-acp reductase (inha) in complex with an… · 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 1ZID · PDBe 1ZID · UniProt P0A5Y6
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