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PDBe Entry: 1e33 view

CRYSTAL STRUCTURE OF AN ARYLSULFATASE A MUTANT P426L
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.5 Å, R-factor: 18.7%, Free R-factor: 25.0%, Spacegroup: I 4 2 2
Released 25/05/2001, deposition: 06/06/2000, last revision: 16/06/2009
Authors Von Buelow, R.search; Schmidt, B.search; Dierks, T.search; Von Figura, K.search; Uson, I.search
Primary citation Defective Oligomerization of Arylsulfatase a as a Cause of its Instability in Lysosomes and Metachromatic Leukodystrophy.
J.BIOL.CHEM.search vol:277, pag:9455-9461 (2002) [PubMed ID 11777924 ]search
Keywords HYDROLASEsearch, CEREBROSIDE-3-SULFATE HYDROLYSISsearch, LYSOSOMAL ENZYMEsearch, FORMYLGLYCINEsearch
EC 3.1.6.8 ExPASy BRENDA search (P)
Organism Homo sapiens(human) 9606search(P)
UniProt Arylsulfatase A precursor (EC 3.1.6.8) (ASA) (Cerebroside-sulfatase) [Contains: Arylsulfatase A component B; Arylsulfatase A component C] P15289search (P)
Solvent P
Related entries 1auk, 1e3c, 1e2s
Polymers
Id Name Type UniProt Residues Observed
P ARYLSULFATASE A Protein P15289 (ARSA_HUMAN)search
489 98%
Heterogens
Id Name Ligands
P SUGAR (2-MER) NDG search
P MAGNESIUM ION MG search
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