MolNFT v1 · #14501 · protein
Oxidoreductase
1MBB · Uridine diphospho-N-acetylenolpyruvylglucosamine reductase: “Oxidoreductase”. X-ray diffraction, 2 ligands (EEB, FAD), 2 pockets (best druggability 0.83). MolNFT v1 #14501 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1MBB
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uridine diphospho-N-acetylenolpyruvylglucosamine reductase
- EC
- 1.1.1.158
- UniProt
- P08373
- Ligands
- EEB, FAD
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uridine diphospho-N-acetylenolpyruvylglucosamine reductase (EC 1.1.1.158) | protein | 340 | 29% helix, 29% strand | P08373 |
Ligands and binding sites
- EEB · Uridine-diphosphate-3(N-acetylglucosaminyl)butyric acid · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
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 | 828 | 0.83 | 0.86 | 85 | EEB, FAD |
| 2 | 73 | 0.31 | 0.74 | 17 | empty |
Compared structures
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 P08373
- Elsewhere: RCSB PDB 1MBB · PDBe 1MBB · UniProt P08373
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