Research workbench
Crystal structure of enoyl-acp reductase from acinetobacter baumannii in complex with NAD and triclosan
Analyse Crystal structure of enoyl-acp reductase from acinetobacter baumannii in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AH9
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- 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
- A0A2J1CZK4
- Ligands
- NAD, TCL
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9) | protein | 260 | 50% helix, 13% strand | A0A2J1CZK4 |
Ligands and binding sites
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 | 541 | 0.78 | 0.85 | 45 | NAD, TCL |
| 2 | 56 | 0.32 | 0.77 | 14 | empty |
Compared structures
- 6AH9 · Crystal structure of enoyl-ACP reductase from Acinetobacter baumannii in complex with NAD… · 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 A0A2J1CZK4
- Elsewhere: RCSB PDB 6AH9 · PDBe 6AH9 · UniProt A0A2J1CZK4
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