Research workbench
X-ray structure of escherichia COLI enoyl reductase with bound NAD and benzo-diazaborine
Analyse X-ray structure of escherichia COLI enoyl reductase with bound NAD and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DFG
- 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
- EC
- 1.3.1.9
- UniProt
- P29132
- Ligands
- NAD, NDT
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enoyl acyl carrier protein reductase (EC 1.3.1.9) | protein | 257 | 49% helix, 15% strand | P29132 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- NDT · 2-(toluene-4-sulfonyl)-2H-benzo[d][1,2,3]diazaborinin-1-ol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 653 | 0.74 | 0.80 | 47 | NAD, NDT |
| 2 | 673 | 0.74 | 0.80 | 53 | NAD, NDT |
| 3 | 113 | 0.48 | 0.80 | 28 | empty |
| 4 | 87 | 0.39 | 0.77 | 14 | empty |
| 5 | 78 | 0.37 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1721 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 1DFG · X-ray structure of escherichia COLI enoyl reductase with bound NAD and benzo-diazaborine · 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 P29132
- Elsewhere: RCSB PDB 1DFG · PDBe 1DFG · UniProt P29132
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