Research workbench
Crystal structure of E.COLI enoyl reductase in complex with NAD and afn-1252
Analyse Crystal structure of E.COLI enoyl reductase in complex with NAD and afn-1252 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JQC
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-[acyl-carrier-protein] reductase [NADH] fabi
- EC
- 1.3.1.9
- UniProt
- P0AEK4
- Ligands
- NAD, 0WE
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-[acyl-carrier-protein] reductase [NADH] fabi (EC 1.3.1.9) | protein | 258 | 48% helix, 16% strand | P0AEK4 |
| B | Enoyl-[acyl-carrier-protein] reductase [NADH] fabi (EC 1.3.1.9) | protein | 256 | 44% helix, 14% strand | P0AEK4 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- 0WE · N-methyl-N-[(3-methyl-1-benzofuran-2-yl)methyl]-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) propanamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 687 | 0.79 | 0.83 | 67 | NAD, 0WE |
| 2 | 656 | 0.78 | 0.83 | 54 | NAD, 0WE |
| 3 | 114 | 0.40 | 0.76 | 17 | empty |
| 4 | 67 | 0.32 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1736 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 4JQC · Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AFN-1252 · the same entry in another collection · chain A against A, TM-score 1.00
- P0AEK4 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH] fabi… · a predicted model of the same protein · chain A 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 P0AEK4
- Elsewhere: RCSB PDB 4JQC · PDBe 4JQC · UniProt P0AEK4
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