Uniprot accession / id : P31428  OR   Uniprot accession / id : P16444
 
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Entry Information
Entry status  (1)
REL
(2)
 
Experimental methods  (1)
X-ray diffraction
(2)
 
Authors  (4)
Adachi H
(2)
Nitanai Y
(2)
Satow Y
(2)
Tsujimoto M
(2)
 
Homo / hetero assembly  (1)
homo
(2)
 
Assembly composition  (1)
protein structure
(2)
 
Assembly polymer count  (1)
dimer
(2)
 
Resolution distribution
1.5 - 2
(1)
2.0 - 2.5
(1)
 
Release year distribution
2000 - 2005
(2)
 
Journal  (1)
J Mol Biol
(2)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(2)
 
Organism name  (1)
Homo sapiens
(2)
 
Molecule name  (6)
Beta-lactamase
(2)
Dehydropeptidase-I
(2)
Dipeptidase 1
(2)
Microsomal dipeptidase
(2)
Renal dipeptidase
(2)
hRDP
(2)
 
Molecule type  (1)
Protein
(2)
 
Gene names  (3)
DPEP1
(2)
MDP
(2)
RDP
(2)
 
Interacting ligands  (3)
NAG : 2-acetamido-2-deoxy-beta-D-glucopyranose
(2)
ZN : ZINC ION
(2)
CIL : CILASTATIN
(1)
 
Function and Biology
EC number / name  (2)
3.4.13.19 : Membrane dipeptidase
(2)
3.5.2.6 : Beta-lactamase
(2)
 
Biological function  (12)
GPI anchor binding
(2)
beta-lactamase activity
(2)
dipeptidase activity
(2)
hydrolase activity
(2)
metal ion binding
(2)
metallodipeptidase activity
(2)
metalloexopeptidase activity
(2)
metallopeptidase activity
(2)
modified amino acid binding
(2)
peptidase activity
(2)
protein binding
(2)
zinc ion binding
(2)
 
Biological process  (14)
antibiotic metabolic process
(2)
cellular response to calcium ion
(2)
cellular response to nitric oxide
(2)
glutathione catabolic process
(2)
glutathione metabolic process
(2)
homocysteine metabolic process
(2)
inflammatory response
(2)
lactam catabolic process
(2)
leukotriene D4 catabolic process
(2)
leukotriene metabolic process
(2)
lipid metabolic process
(2)
negative regulation of cell migration
(2)
neutrophil chemotaxis
(2)
proteolysis
(2)
 
Biological cell component  (11)
apical part of cell
(2)
apical plasma membrane
(2)
cell junction
(2)
cell projection
(2)
extracellular exosome
(2)
extracellular space
(2)
membrane
(2)
microvillus membrane
(2)
nucleoplasm
(2)
plasma membrane
(2)
side of membrane
(2)
 
Sequence and Structure classification
SCOP fold  (1)
TIM beta/alpha-barrel
(2)
 
SCOP family  (1)
Renal dipeptidase
(2)
 
CATH class  (1)
Alpha Beta
(2)
 
CATH topology  (1)
TIM Barrel
(2)
 
Pfam accession / name  (1)
PF01244 : Peptidase_M19
(2)
 
Experimental Information
Diffraction protocol  (1)
Single wavelength
(2)
 
Diffraction radiation source type  (1)
Rotating anode
(2)
 
Diffraction source  (1)
RIGAKU RU300
(2)
 
Diffraction detector type  (1)
Image plate
(2)
 
Refinement software  (1)
X-PLOR
(2)
 
Representative Structures
Representative Structures
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Entries 1 to 2 of 2
Entries 1 to 2 of 2
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HUMAN RENAL DIPEPTIDASE COMPLEXED WITH CILASTATIN
Nitanai Y, Satow Y, Adachi H, Tsujimoto M
J Mol Biol (2002) [PMID: 12144777  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: CIL    NAG    ZN    ZN    NAG    CIL   
Assembly name: Dipeptidase 1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-147727 (Preferred)   search this ID
PDBe-KB: P16444   
X-ray diffraction
2Å resolution
Released: 28 Aug 2002
Model geometry
Fit model/data
1itu
1itu
1itu
HUMAN RENAL DIPEPTIDASE
Nitanai Y, Satow Y, Adachi H, Tsujimoto M
J Mol Biol (2002) [PMID: 12144777  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: NAG    ZN    ZN    NAG   
Assembly name: Dipeptidase 1 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-147727 (Preferred)   search this ID
PDBe-KB: P16444   
X-ray diffraction
2.3Å resolution
Released: 28 Aug 2002
Model geometry
Fit model/data
1itq
1itq
1itq
Entries 1 to 2 of 2
Entries 1 to 2 of 2