Human brain aspartoacylase mutant Y231C complex with intermediate analog (N-phosphonomethyl-L-aspartate)

Summary for 4TNU

DescriptorAspartoacylase, ZINC ION, N-[HYDROXY(METHYL)PHOSPHORYL]-L-ASPARTIC ACID, ... (4 entities in total)
Functional Keywordscanavan disease, zinc-dependent hydrolase, aspartoacylase family, aminoacylase-2, n-acetyl-l-aspartate, hydrolase
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm P45381
Total number of polymer chains2
Total molecular weight72001.14
Wijayasinghe, Y.S.,Pavlovsky, A.G.,Viola, R.E. (deposition date: 2014-06-05, release date: 2014-07-30, Last modification date: 2014-10-01)
Primary citation
Wijayasinghe, Y.S.,Pavlovsky, A.G.,Viola, R.E.
Aspartoacylase catalytic deficiency as the cause of canavan disease: a structural perspective.
Biochemistry, 53:4970-4978, 2014
PubMed: 25003821 (PDB entries with the same primary citation)
DOI: 10.1021/bi500719k
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.22740.3%2.3%0.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload