3N2Z
The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution
Summary for 3N2Z
Entry DOI | 10.2210/pdb3n2z/pdb |
Related | 3JYH |
Descriptor | Lysosomal Pro-X carboxypeptidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | alpha/beta hydrolase, prcp, serine carboxypeptidase, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Lysosome: P42785 |
Total number of polymer chains | 1 |
Total formula weight | 51976.46 |
Authors | Soisson, S.M.,Patel, S.B.,Lumb, K.J.,Sharma, S. (deposition date: 2010-05-19, release date: 2010-07-07, Last modification date: 2024-10-16) |
Primary citation | Soisson, S.M.,Patel, S.B.,Abeywickrema, P.D.,Bryne, N.J.,Diehl, R.E.,Hall, D.L.,Ford, R.E.,Reid, J.C.,Rickert, K.W.,Shipman, J.M.,Sharma, S.,Lumb, K.J. Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase. Bmc Struct.Biol., 10:16-16, 2010 Cited by PubMed Abstract: The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7. The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described. PubMed: 20540760DOI: 10.1186/1472-6807-10-16 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.79 Å) |
Structure validation
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