Research workbench
E. COLI dihydroorotate dehydrogenase bound to the inhibitor hqno
Analyse E. COLI dihydroorotate dehydrogenase bound to the inhibitor hqno in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T5K
- Type
- protein
- Length
- 670 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydroorotate dehydrogenase (quinone)
- EC
- 1.3.5.2
- UniProt
- P0A7E1
- Ligands
- FMN, HQO, ORO
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) | protein | 335 | 43% helix, 17% strand | P0A7E1 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- HQO · 2-heptyl-4-hydroxy quinoline N-oxide · ligand · 2 copies · chains A, B
- ORO · Orotic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 614 | 0.81 | 0.86 | 82 | FMN, HQO, ORO |
| 2 | 563 | 0.81 | 0.87 | 72 | HQO, FMN, ORO |
| 3 | 404 | 0.62 | 0.77 | 37 | empty |
| 4 | 58 | 0.35 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 956 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 7T5K · E. coli dihydroorotate dehydrogenase bound to the inhibitor HQNO · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7E1 · AlphaFold monomer V2.0 prediction for dihydroorotate dehydrogenase (quinone) (P0A7E1) · 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 P0A7E1
- Elsewhere: RCSB PDB 7T5K · PDBe 7T5K · UniProt P0A7E1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.