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3GHH

Structural insights into the catalytic mechanism of CD38: Evidence for a conformationally flexible covalent enzyme-substrate complex.

Summary for 3GHH
Entry DOI10.2210/pdb3ghh/pdb
Related1YH3 3GC6 3GH3
DescriptorEcto-NAD+ glycohydrolase (CD38 molecule), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total)
Functional Keywordscd38, cyclic adp ribose, ecto-adp-ribosyl cyclase, 2-glycosidase, glycosidase, hydrolase
Biological sourceBos taurus (bovine,cow,domestic cattle,domestic cow)
Total number of polymer chains2
Total formula weight58594.66
Authors
Egea, P.F.,Muller-Steffner, H.,Stroud, R.M.,Oppenheimer, N.J.,Kellenberger, E.,Schuber, F. (deposition date: 2009-03-03, release date: 2010-03-16, Last modification date: 2023-09-06)
Primary citationEgea, P.F.,Muller-Steffner, H.,Kuhn, I.,Cakir-Kiefer, C.,Oppenheimer, N.J.,Stroud, R.M.,Kellenberger, E.,Schuber, F.
Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the X-ray structures of its Michaelis complex and covalently-trapped intermediates.
Plos One, 7:e34918-e34918, 2012
Cited by
PubMed: 22529956
DOI: 10.1371/journal.pone.0034918
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

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