Structure of PDB 1itu Chain B Binding Site BS02

Receptor Information
>1itu Chain B (length=369) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHT
NIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETF
LYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTL
THSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVS
VATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVN
FYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLE
DVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLTQAPEEE
PIPLDQLGGSCRTHYGYSS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1itu Chain B Residue 412 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1itu Crystal Structure of Human Renal Dipeptidase Involved in beta-Lactam Hydrolysis
Resolution2.0 Å
Binding residue
(original residue number in PDB)		E125 H198 H219
Binding residue
(residue number reindexed from 1)		E125 H198 H219
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H20 D22 E125 H152 H198 H219 D288
Catalytic site (residue number reindexed from 1) H20 D22 E125 H152 H198 H219 D288
Enzyme Commision number 3.4.13.19: membrane dipeptidase.
3.5.2.6: beta-lactamase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008235 metalloexopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016805 dipeptidase activity
GO:0034235 GPI anchor binding
GO:0043027 cysteine-type endopeptidase inhibitor activity involved in apoptotic process
GO:0046872 metal ion binding
GO:0070573 metallodipeptidase activity
GO:0072341 modified amino acid binding
Biological Process
GO:0006508 proteolysis
GO:0006629 lipid metabolic process
GO:0006691 leukotriene metabolic process
GO:0006749 glutathione metabolic process
GO:0006751 glutathione catabolic process
GO:0006954 inflammatory response
GO:0016999 antibiotic metabolic process
GO:0030336 negative regulation of cell migration
GO:0030593 neutrophil chemotaxis
GO:0043066 negative regulation of apoptotic process
GO:0043154 negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0050667 homocysteine metabolic process
GO:0071277 cellular response to calcium ion
GO:0071466 cellular response to xenobiotic stimulus
GO:0071732 cellular response to nitric oxide
GO:0072340 lactam catabolic process
GO:1901749 leukotriene D4 catabolic process
Cellular Component
GO:0005615 extracellular space
GO:0005654 nucleoplasm
GO:0005886 plasma membrane
GO:0016324 apical plasma membrane
GO:0030054 cell junction
GO:0031528 microvillus membrane
GO:0042995 cell projection
GO:0045177 apical part of cell
GO:0070062 extracellular exosome
GO:0098552 side of membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1itu, PDBe:1itu, PDBj:1itu
PDBsum1itu
PubMed12144777
UniProtP16444|DPEP1_HUMAN Dipeptidase 1 (Gene Name=DPEP1)

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