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1P52

Structure of Arginine kinase E314D mutant

Summary for 1P52
Entry DOI10.2210/pdb1p52/pdb
Related1BG0
DescriptorArginine kinase, NITRATE ION, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsarginine kinase, phosphagen kinase, transition state analog, adenosine tri-phosphate, transferase
Biological sourceLimulus polyphemus (Atlantic horseshoe crab)
Cellular locationCytoplasm: P51541
Total number of polymer chains1
Total formula weight41044.49
Authors
Pruett, P.S.,Azzi, A.,Clark, S.A.,Yousef, M.S.,Gattis, J.L.,Somasundarum, T.,Ellington, W.R.,Chapman, M.S. (deposition date: 2003-04-24, release date: 2003-06-17, Last modification date: 2023-08-16)
Primary citationPruett, P.S.,Azzi, A.,Clark, S.A.,Yousef, M.S.,Gattis, J.L.,Somasundaram, T.,Ellington, W.R.,Chapman, M.S.
The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
J.Biol.Chem., 278:26952-26957, 2003
Cited by
PubMed: 12732621
DOI: 10.1074/jbc.M212931200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

221051

数据于2024-06-12公开中

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