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Structure paper

TitleAspartoacylase catalytic deficiency as the cause of canavan disease: a structural perspective.
Journal, issue, pagesBiochemistry, Vol. 53, Page 4970-4978, Year 2014
Publish dateSep 17, 2013 (structure data deposition date)
AuthorsWijayasinghe, Y.S. / Pavlovsky, A.G. / Viola, R.E.
External linksBiochemistry / PubMed:25003821
MethodsX-ray diffraction
Resolution2.6 - 3 Å
Structure data

PDB-4mri:
Human brain aspartoacylase mutant F295S complex with intermediate analog (N-phosphonomethyl-L-aspartate)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4mxu:
Human brain aspartoacylase mutant K213E complex with intermediate analog (N-phosphonomethyl-L-aspartate)
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-4nfr:
Human brain aspartoacylase mutant E285A complex with intermediate analog (N-phosphonomethyl-L-aspartate)
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-4tnu:
Human brain aspartoacylase mutant Y231C complex with intermediate analog (N-phosphonomethyl-L-aspartate)
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-AS9:
N-[HYDROXY(METHYL)PHOSPHORYL]-L-ASPARTIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Canavan disease / N-acetyl-L-aspartate / Zinc-dependent hydrolase / aspartoacylase family / aminoacylase-2

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