MolNFT v1 · #27379 · protein
Quinone reductase 2 in complex with cancer prodrug CB1954
1XI2 · Nrh dehydrogenase [quinone] 2: “Quinone reductase 2 in complex with cancer prodrug CB1954”. X-ray diffraction, 3 ligands (FAD, CB1, ZN), 2 pockets (best druggability 0.77). MolNFT v1 #27379 on GenesisL1: 3D structure, binding sites…
- PDB
- 1XI2
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nrh dehydrogenase [quinone] 2
- EC
- 1.6.99.-
- UniProt
- P16083
- Ligands
- FAD, CB1, ZN
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nrh dehydrogenase [quinone] 2 (EC 1.6.99.-) | protein | 230 | 39% helix, 16% strand | P16083 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- CB1 · 5-(aziridin-1-yl)-2,4-dinitrobenzamide · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 3 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 | 568 | 0.77 | 0.83 | 48 | FAD, CB1 |
| 2 | 600 | 0.75 | 0.82 | 45 | FAD, CB1 |
Interfaces
1 interface between chains.
- A–B · 2019 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1XI2 · Qui Reductase 2 in Complex with Cancer Prodrug CB1954 · the same entry in another collection · chain A against A, TM-score 1.00
- P16083 · AlphaFold monomer V2.0 prediction for ribosyldihydronicotinamide dehydrogenase [quinone]… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 1XI2 · PDBe 1XI2 · UniProt P16083
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