1F76: Escherichia Coli Dihydroorotate Dehydrogenase

Citation:
Abstract
The flavoenzymes dihydroorotate dehydrogenases (DHODs) catalyze the fourth and only redox step in the de novo biosynthesis of UMP. Enzymes belonging to class 2, according to their amino acid sequence, are characterized by having a serine residue as the catalytic base and a longer N terminus. The structure of class 2 E. coli DHOD, determined by MAD phasing, showed that the N-terminal extension forms a separate domain. The catalytic serine residue has an environment differing from the equivalent cysteine in class 1 DHODs. Significant differences between the two classes of DHODs were identified by comparison of the E. coli DHOD with the other known DHOD structures, and differences with the class 2 human DHOD explain the variation in their inhibitors.
PDB ID: 1F76Download
MMDB ID: 20764
PDB Deposition Date: 2000/6/26
Updated in MMDB: 2002/11
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 1F76: monomeric; determined by author
Molecular Components in 1F76
Label Count Molecule
Protein (1 molecule)
1
Dihydroorotate Dehydrogenase (Quinone)(Gene symbol: pyrD)
Molecule annotation
Chemicals (3 molecules)
1
1
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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