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Ligands
Code Name Style Show Link
MN Manganese (II) ion
PI Hydrogenphosphate ion
Non-standard Residues
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Glycosylation
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Code : 2OKN   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal Strcture of Human Prolidase
Release Data : 2007-02-20
Compound :
mol_id molecule chains synonym
1 Xaa-Pro dipeptidase A,B X-Pro dipeptidase, Proline dipeptidase, Prolidase, Imidodipeptidase
ec: 3.4.13.9
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: PEPD, PRD
expression_system_strain: SCS1/PRARE
expression_system_vector_type: PLASMID
expression_system_plasmid: RZPD CLONE ID PSFEP250H122
Authors : Mueller, U., Niesen, F.H., Roske, Y., Goetz, F., Behlke, J., Buessow, K., Heinemann, U., Protein Structure Factory (PSF)
Keywords : METALLOCARBOXYPEPTIDASE, DISEASE MUTATION, XAA-PRO DIPEPTIDASE, DIPEPTIDASE, PEPTIDASE D, COLLAGEN DEGRADATION, METALLOAMINOPEPTIDASE, ENZYME, PROTEASE, PEPD GENE, MANGANESE, HYDROLASE, METAL-BINDING, METALLOPROTEASE, PHOSPHORYLATION, Structural Genomics, Protein Structure Factory, PSF
Exp. method : X-RAY DIFFRACTION ( 2.450 Å )
Citation :

Crystal Structure of Human Prolidase: The Molecular Basis of PD Disease.

MUELLER, U.,NIESEN, F.H.,ROSKE, Y.  et al.
To be Published 

Chain : A, B
UniProt : P12955 (PEPD_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline 3.4.13.9 PubMed:17081196, PubMed:35165443
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