1f76
From Proteopedia
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|PDB= 1f76 |SIZE=350|CAPTION= <scene name='initialview01'>1f76</scene>, resolution 2.5Å | |PDB= 1f76 |SIZE=350|CAPTION= <scene name='initialview01'>1f76</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydroorotate_oxidase Dihydroorotate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.1 1.3.3.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotate_oxidase Dihydroorotate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.1 1.3.3.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f76 OCA], [http://www.ebi.ac.uk/pdbsum/1f76 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f76 RCSB]</span> | ||
}} | }} | ||
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[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
[[Category: Norager, S.]] | [[Category: Norager, S.]] | ||
| - | [[Category: FMN]] | ||
| - | [[Category: FMT]] | ||
| - | [[Category: ORO]] | ||
[[Category: alpha-beta-barrel]] | [[Category: alpha-beta-barrel]] | ||
[[Category: fmn binding domain]] | [[Category: fmn binding domain]] | ||
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[[Category: orotate complex]] | [[Category: orotate complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:17:14 2008'' |
Revision as of 17:17, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Dihydroorotate oxidase, with EC number 1.3.3.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE
Overview
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.
About this Structure
1F76 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases., Norager S, Jensen KF, Bjornberg O, Larsen S, Structure. 2002 Sep;10(9):1211-23. PMID:12220493 [[Category: ]]
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