1NM8

Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer

Summary for 1NM8

DescriptorCarnitine O-acetyltransferase (2 entities in total)
Functional Keywordstwo equally sized domains, anti-parallel beta-strand, transferase
Biological sourceHomo sapiens (human)
Cellular locationEndoplasmic reticulum (Potential). Isoform 1: Mitochondrion (Potential). Isoform 2: Peroxisome (Potential) P43155
Total number of polymer chains1
Total molecular weight69902.87
Authors
Wu, D.,Govindasamy, L.,Lian, W.,Gu, Y.,Kukar, T.,Agbandje-McKenna, M.,McKenna, R. (deposition date: 2003-01-09, release date: 2003-03-11, Last modification date: 2011-07-13)
Primary citation
Wu, D.,Govindasamy, L.,Lian, W.,Gu, Y.,Kukar, T.,Agbandje-McKenna, M.,McKenna, R.
Structure of Human Carnitine Acetyltransferase. Molecular Basis for Fatty Acyl Transfer
J.Biol.Chem., 278:13159-13165, 2003
PubMed: 12562770 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M212356200
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.6 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.262110.5%1.9%8.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution