MolNFT v1 · #3826 · protein
Crystal structure of human NAD[P]H-quinone oxidoreductase at 1.7 a resolution
1D4A · Quinone reductase: “Crystal structure of human NAD[P]H-quinone oxidoreductase at 1.7 a resolution”. X-ray diffraction, 1 ligand (FAD), 7 pockets (best druggability 0.79). MolNFT v1 #3826 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1D4A
- Type
- protein
- Length
- 1,092 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Quinone reductase
- EC
- 1.6.99.2
- UniProt
- P15559
- Ligands
- FAD
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Quinone reductase (EC 1.6.99.2) | protein | 273 | 40% helix, 16% strand | P15559 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.79 | 0.98 | 19 | empty |
| 2 | 97 | 0.77 | 0.98 | 20 | empty |
| 3 | 583 | 0.77 | 0.83 | 51 | FAD |
| 4 | 569 | 0.77 | 0.83 | 52 | FAD |
| 5 | 526 | 0.76 | 0.83 | 49 | FAD |
Interfaces
2 interfaces between chains.
- A–C · 2824 Ų buried · 33 hydrogen bonds · protein-protein
- B–D · 2745 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 1D4A · Crystal structure of human NAD[P]H-quinone oxidoreductase at 1.7 a resolution · the same entry in another collection · chain B against B, TM-score 1.00
- P15559 · AlphaFold monomer V2.0 prediction for NAD(P)H dehydrogenase [quinone] 1 (P15559) · 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 P15559
- Elsewhere: RCSB PDB 1D4A · PDBe 1D4A · UniProt P15559
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.