3A6D

Creatininase complexed with 1-methylguanidine

Summary for 3A6D

Related1J2T 1J2U 1V7Z 3A6E 3A6F 3A6G 3A6H
DescriptorCreatinine amidohydrolase, MANGANESE (II) ION, ZINC ION, ... (6 entities in total)
Functional Keywordscreatinine amidohydrolase, urease-related amidohydrolase superfamily, closed form, hydrolase
Biological sourcePseudomonas putida
Total number of polymer chains6
Total molecular weight174482.53
Authors
Nakajima, Y.,Yamashita, K.,Ito, K.,Yoshimoto, T. (deposition date: 2009-08-31, release date: 2010-02-09, Last modification date: 2014-01-22)
Primary citation
Yamashita, K.,Nakajima, Y.,Matsushita, H.,Nishiya, Y.,Yamazawa, R.,Wu, Y.F.,Matsubara, F.,Oyama, H.,Ito, K.,Yoshimoto, T.
Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase
J.Mol.Biol., 396:1081-1096, 2010
PubMed: 20043918 (PDB entries with the same primary citation)
DOI: 10.1016/j.jmb.2009.12.045
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.9 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.207400.6%3.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution