Research workbench
X-ray structure of escherichia COLI enoyl reductase with bound NAD and thieno-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
- 1DFH
- 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, TDB
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Enoyl acyl carrier protein reductase (EC 1.3.1.9) | protein | 257 | 48% helix, 16% strand | P29132 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- TDB · 6-methyl-2(propane-1-sulfonyl)-2H-thieno[3,2-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 | 713 | 0.75 | 0.80 | 50 | NAD, TDB |
| 2 | 658 | 0.75 | 0.81 | 46 | NAD, TDB |
| 3 | 91 | 0.40 | 0.77 | 21 | empty |
| 4 | 91 | 0.38 | 0.77 | 14 | empty |
| 5 | 99 | 0.36 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1754 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 1DFH · X-ray structure of escherichia COLI enoyl reductase with bound NAD and thieno-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 1DFH · PDBe 1DFH · UniProt P29132
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