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3E2P

Catalytic subunit of M. Jannaschii aspartate transcarbamoylase in an orthorhombic crystal form

Summary for 3E2P
Entry DOI10.2210/pdb3e2p/pdb
DescriptorAspartate carbamoyltransferase, SULFATE ION (3 entities in total)
Functional Keywordsaspartate transcarbamoylase, atcase, pyrimidine biosynthesis, thermostability, methanococcus jannaschii, transferase
Biological sourceMethanocaldococcus jannaschii (Methanococcus jannaschii)
Total number of polymer chains12
Total formula weight422911.70
Authors
Vitali, J.,Colaneri, M.J. (deposition date: 2008-08-06, release date: 2009-03-10, Last modification date: 2023-08-30)
Primary citationVitali, J.,Colaneri, M.J.
Structure of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form.
Acta Crystallogr.,Sect.F, 64:776-780, 2008
Cited by
PubMed Abstract: Crystals of the catalytic subunit of Methanococcus jannaschii aspartate transcarbamoylase in an orthorhombic crystal form contain four crystallographically independent trimers which associate in pairs to form stable staggered complexes that are similar to each other and to a previously determined monoclinic C2 form. Each subunit has a sulfate in the central channel. The catalytic subunits in these complexes show flexibility, with the elbow angles of the monomers differing by up to 7.4 degrees between crystal forms. Moreover, there is also flexibility in the relative orientation of the trimers around their threefold axis in the complexes, with a difference of 4 degrees between crystal forms.
PubMed: 18765902
DOI: 10.1107/S1744309108025359
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

237992

数据于2025-06-25公开中

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