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: 19301871DOI: 10.1021/bi900220s PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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