MolNFT v1 · #125539 · protein
Structure of the human quinone reductase 2 (NQO2) in complex with imiquimod
5LBT: “Structure of the human quinone reductase 2 (NQO2) in complex with imiquimod”. X-ray diffraction, 4 ligands (6T0, FAD, ZN). MolNFT v1 #125539 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LBT
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16083
- Ligands
- 6T0, FAD, ZN, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 228 | — | P16083 |
| B | — | protein | 226 | — | P16083 |
Ligands and binding sites
- 6T0 · 1-(2-methylpropyl)imidazo[4,5-c]quinolin-4-amine · ligand · 4 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LBT · Structure of the human qui reductase 2 (NQO2) in complex with imiquimod · 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 P16083
- Elsewhere: RCSB PDB 5LBT · PDBe 5LBT · UniProt P16083
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