MolNFT v1 · #125540 · protein
Structure of the human quinone reductase 2 (NQO2) in complex with to CL097
5LBU · Ribosyldihydronicotinamide dehydrogenase [quinone]: “Structure of the human quinone reductase 2 (NQO2) in complex with to CL097”. X-ray diffraction, 4 ligands (C09, FAD, ZN), 2 pockets (best druggability 0.78). MolNFT v1 #125540 on…
- PDB
- 5LBU
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosyldihydronicotinamide dehydrogenase [quinone]
- EC
- 1.10.5.1
- UniProt
- P16083
- Ligands
- C09, FAD, ZN, SO4
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribosyldihydronicotinamide dehydrogenase [quinone] (EC 1.10.5.1) | protein | 228 | 42% helix, 16% strand | P16083 |
Ligands and binding sites
- C09 · 2-(ethoxymethyl)-1H-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 · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 569 | 0.78 | 0.84 | 43 | C09, FAD |
| 2 | 549 | 0.78 | 0.84 | 42 | FAD, C09 |
Interfaces
1 interface between chains.
- A–B · 2042 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 5LBU · Structure of the human qui reductase 2 (NQO2) in complex with to CL097 · 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 5LBU · PDBe 5LBU · UniProt P16083
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.