3BXM

Structure of an inactive mutant of human glutamate carboxypeptidase II [GCPII(E424A)] in complex with N-acetyl-Asp-Glu (NAAG)

Summary for 3BXM

Entry DOI	10.2210/pdb3bxm/pdb
Descriptor	Glutamate carboxypeptidase 2, N-Acetyl-Aspartyl-Glutamate (NAAG), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
Functional Keywords	protein-substrate complex, carboxypeptidase, dipeptidase, glycoprotein, hydrolase, membrane, metal-binding, metalloprotease, multifunctional enzyme, protease, signal-anchor, transmembrane
Biological source	Homo sapiens (human) More
Cellular location	Cell membrane; Single-pass type II membrane protein. Isoform PSMA': Cytoplasm: Q04609
Total number of polymer chains	2
Total formula weight	82981.10
Authors	Lubkowski, J.,Barinka, C. (deposition date: 2008-01-14, release date: 2009-01-27, Last modification date: 2023-08-30)
Primary citation	Klusak, V.,Barinka, C.,Plechanovova, A.,Mlcochova, P.,Konvalinka, J.,Rulisek, L.,Lubkowski, J. Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods. Biochemistry, 48:4126-4138, 2009 Cited by PubMed: 19301871 DOI: 10.1021/bi900220s PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.71 Å)

Structure validation