3D6N
Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase
Summary for 3D6N
Entry DOI | 10.2210/pdb3d6n/pdb |
Related | 1xrf 1xrt |
Descriptor | Dihydroorotase, Aspartate carbamoyltransferase, ZINC ION, ... (5 entities in total) |
Functional Keywords | reactor, chamber, pores, internal cavity, hydrolase, metal-binding, pyrimidine biosynthesis, transferase, hydrolase-transferase complex, hydrolase/transferase |
Biological source | Aquifex aeolicus More |
Total number of polymer chains | 2 |
Total formula weight | 80490.88 |
Authors | Edwards, B.F.P. (deposition date: 2008-05-20, release date: 2009-01-20, Last modification date: 2023-08-30) |
Primary citation | Zhang, 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: 19128030DOI: 10.1021/bi801831r PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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