MolNFT v1 · #89837 · protein
Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase
4E13: “Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase”. X-ray diffraction, 2 ligands (NAD, SO4), 1 pocket (best druggability 0.58). MolNFT v1 #89837 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4E13
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diketoreductase
- UniProt
- B1P3E1
- Ligands
- NAD, SO4
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diketoreductase | protein | 283 | 50% helix, 14% strand | B1P3E1 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 4 copies · chains A
- 1PE · Pentaethylene glycol · additive · 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 | 326 | 0.58 | 0.76 | 43 | NAD, GOL, 1PE |
Compared structures
- 4E13 · Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase · 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 B1P3E1
- Elsewhere: RCSB PDB 4E13 · PDBe 4E13 · UniProt B1P3E1
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