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3D6N

Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase

Summary for 3D6N
Entry DOI10.2210/pdb3d6n/pdb
Related1xrf 1xrt
DescriptorDihydroorotase, Aspartate carbamoyltransferase, ZINC ION, ... (5 entities in total)
Functional Keywordsreactor, chamber, pores, internal cavity, hydrolase, metal-binding, pyrimidine biosynthesis, transferase, hydrolase-transferase complex, hydrolase/transferase
Biological sourceAquifex aeolicus
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Total number of polymer chains2
Total formula weight80490.88
Authors
Edwards, B.F.P. (deposition date: 2008-05-20, release date: 2009-01-20, Last modification date: 2023-08-30)
Primary citationZhang, P.,Martin, P.D.,Purcarea, C.,Vaishnav, A.,Brunzelle, J.S.,Fernando, R.,Guy-Evans, H.I.,Evans, D.R.,Edwards, B.F.
Dihydroorotase from the hyperthermophile Aquifiex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis.
Biochemistry, 48:766-778, 2009
Cited by
PubMed: 19128030
DOI: 10.1021/bi801831r
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

218500

数据于2024-04-17公开中

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