Brand  (β version)

PDB ID: 1ITU

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Ligands
Code Name Style Show Link
CIL Cilastatin PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
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Structure summary

Code : 1ITU   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : HUMAN RENAL DIPEPTIDASE COMPLEXED WITH CILASTATIN
Release Data : 2002-08-28
Compound :
mol_id molecule chains synonym
1 RENAL DIPEPTIDASE A,B Microsomal dipeptidase
ec: 3.4.13.19
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Pichia pastoris  (taxid:4922)
tissue: renal cortex
expression_system_strain: GS115
expression_system_vector_type: plasmid
expression_system_plasmid: PHILD2
Authors : Nitanai, Y., Satow, Y., Adachi, H., Tsujimoto, M.
Keywords : DIPEPTIDASE, GLYCOPROTEIN, MEMBRANE-BOUND, ZINC PROTEASE BETA-LACTAMASE, CILASTATIN, COMPLEX (HYDROLASE-INHIBITOR), HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Crystal Structure of Human Renal Dipeptidase Involved in beta-Lactam Hydrolysis

Nitanai, Y.,Satow, Y.,Adachi, H.  et al.
(2002)  J.Mol.Biol.  321 : 177 - 184

PubMed: 12144777
DOI: 10.1016/S0022-2836(02)00632-0

Crystallization and preliminary X-ray investigation of a glycoprotein, human renal dipeptidase

Nitanai, Y.,Satow, Y.,Adachi, H.  et al.
(1996)  J.CRYST.GROWTH  168 : 280 - 283

DOI: 10.1016/0022-0248(96)00332-6

Reaction

Chain : A, B
UniProt : P16444 (DPEP1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid 3.4.13.19 PROSITE-ProRule:PRU10073, PubMed:2303490, PubMed:32325220
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leukotriene D4 + H2O = leukotriene E4 + glycine - PubMed:2303490, PubMed:32325220
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a beta-lactam + H2O = a substituted beta-amino acid 3.5.2.6 PubMed:32325220, PubMed:6334084
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L-cystine-bis-glycine + 2 H2O = L-cystine + 2 glycine - PubMed:32325220
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glycyldehydrophenylalanine + H2O = 2,3-didehydrophenylalanine + glycine - PubMed:2303490, PubMed:31442408, PubMed:6334084
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Cofactor: Evidence: Note:
Zn(2+) ECO:0000255 | PROSITE-ProRule:PRU10073
ECO:0000269 | PubMed:12144777
Binds 2 Zn(2+) ion per monomer.