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3N2Z

The Structure of Human Prolylcarboxypeptidase at 2.80 Angstroms Resolution

Summary for 3N2Z
Entry DOI10.2210/pdb3n2z/pdb
Related3JYH
DescriptorLysosomal 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 Keywordsalpha/beta hydrolase, prcp, serine carboxypeptidase, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationLysosome: P42785
Total number of polymer chains1
Total formula weight51976.46
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 citationSoisson, 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: 20540760
DOI: 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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