MolNFT v1 · #49403 · protein
Quinone reductase 2 in complex with dopamine
2QMZ · Ribosyldihydronicotinamide dehydrogenase: “Quinone reductase 2 in complex with dopamine”. X-ray diffraction, 3 ligands (FAD, LDP, ZN), 2 pockets (best druggability 0.77). MolNFT v1 #49403 on GenesisL1: 3D structure, binding sites…
- PDB
- 2QMZ
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosyldihydronicotinamide dehydrogenase
- EC
- 1.10.99.2
- UniProt
- P16083
- Ligands
- FAD, LDP, ZN
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ribosyldihydronicotinamide dehydrogenase (EC 1.10.99.2) | protein | 230 | 41% helix, 16% strand | P16083 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- LDP · L-dopamine · 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 | 562 | 0.77 | 0.83 | 46 | FAD, LDP |
| 2 | 571 | 0.76 | 0.82 | 42 | FAD, LDP |
Interfaces
1 interface between chains.
- A–B · 2050 Ų buried · 29 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 2QMZ · PDBe 2QMZ · UniProt P16083
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