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PDBe Entry: 1apz view

HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT
Summary
Header COMPLEX (HYDROLASE/PEPTIDE)search
Method X-RAY DIFFRACTION
Experiment Resolution: 2.3 Å, R-factor: 21.2%, Free R-factor: 29.1%, Spacegroup: P 61
Released 23/12/1996, deposition: 14/06/1995, last revision: 24/02/2009
Authors Rouvinen, J.search; Oinonen, C.search
Primary citation Three-dimensional structure of human lysosomal aspartylglucosaminidase.
NAT.STRUCT.BIOL.search vol:2, pag:1102-1108 (1995) [PubMed ID 8846222 ]search
Keywords ASPARTYLGLUCOSAMINIDASEsearch, GLYCOSYLASPARAGINASEsearch, COMPLEX (HYDROLASE/PEPTIDE)search
EC 3.5.1.26 ExPASy BRENDA search (A B C D)
Organism Homo sapiens(human) 9606search(A C B D)
UniProt N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase precursor (EC 3.5.1.26) (Glycosylasparaginase) (Aspartylglucosaminidase) (AGA) (N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase) [Contains: Glycosylasparaginase alpha chain; Glycosylasparaginase beta chain] P20933search (A C B D)
Solvent A, B, C, D
Polymers
Id Name Type UniProt Residues Observed
A, C ASPARTYLGLUCOSAMINIDASE Protein P20933 (ASPG_HUMAN)search
162 99%
B, D ASPARTYLGLUCOSAMINIDASE Protein P20933 (ASPG_HUMAN)search
141 100%
Heterogens
Id Name Ligands
A, B, C SUGAR (N-ACETYL-D-GLUCOSAMINE) NAG search
D SUGAR (3-MER) NAG search BMA search
B, D ASPARTIC ACID ASP search
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