MolNFT v1 · #19667 · protein
Human quinone reductase type 2
1QR2 · Protein (quinone reductase type 2): “Human quinone reductase type 2”. X-ray diffraction, 2 ligands (FAD, ZN), 2 pockets (best druggability 0.76). MolNFT v1 #19667 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QR2
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (quinone reductase type 2)
- EC
- 1.6.99.2
- UniProt
- P16083
- Ligands
- FAD, ZN
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (quinone reductase type 2) (EC 1.6.99.2) | protein | 230 | 43% helix, 16% strand | P16083 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 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 | 583 | 0.76 | 0.82 | 46 | FAD |
| 2 | 588 | 0.75 | 0.82 | 43 | FAD |
Interfaces
1 interface between chains.
- A–B · 2021 Ų buried · 27 hydrogen bonds · protein-protein
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 P16083
- Elsewhere: RCSB PDB 1QR2 · PDBe 1QR2 · UniProt P16083
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