MolNFT v1 · #73460 · protein
X-ray crystallographic structure activity relationship (sar) of casimiroin and its analogs bound to human quinone reductase 2
3O2N · Ribosyldihydronicotinamide dehydrogenase [quinone]: “X-ray crystallographic structure activity relationship (sar) of casimiroin and its analogs bound to human…”. X-ray diffraction, 3 ligands (MZX, FAD, ZN), 2 pockets (best…
- PDB
- 3O2N
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosyldihydronicotinamide dehydrogenase [quinone]
- EC
- 1.10.99.2
- UniProt
- P16083
- Ligands
- MZX, FAD, ZN
- Pockets
- 2 · best druggability 0.77
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 1.10.99.2) | protein | 230 | 42% helix, 16% strand | P16083 |
Ligands and binding sites
- MZX · 5,8-dimethoxy-4-methylquinolin-2(1H)-one · ligand · 3 copies · chains A, B
- 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 | 586 | 0.77 | 0.83 | 49 | FAD, MZX |
| 2 | 622 | 0.75 | 0.81 | 47 | MZX, FAD |
Interfaces
1 interface between chains.
- A–B · 2046 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 3O2N · X-ray Crystallographic Structure Activity Relationship (SAR) of Casimiroin and its… · 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 3O2N · PDBe 3O2N · UniProt P16083
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