GL1X · GenesisL1 explorer

Research workbench

E. COLI dihydroorotate dehydrogenase bound to the inhibitor hmnq

Analyse E. COLI dihydroorotate dehydrogenase bound to the inhibitor hmnq in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7T5Y
Type
protein
Length
671 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P0A7E1
Ligands
F2D, ORO, FMN, PO4

Structure

x-ray diffraction · 2 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein336—P0A7E1
B—protein335—P0A7E1

Ligands and binding sites

  • F2D · 3-methyl-2-[(2E)-non-2-en-1-yl]quinolin-4(1H)-one · ligand · 2 copies · chains A, B
  • ORO · Orotic acid · ligand · 2 copies · chains A, B
  • FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 7T5Y · E. coli dihydroorotate dehydrogenase bound to the inhibitor HMNQ · 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 B against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.