1itq Summary



The structure was published by Nitanai, Y., Satow, Y., Adachi, H., and Tsujimoto, M., in 2002 in a paper entitled "Crystal Structure of Human Renal Dipeptidase Involved in beta-Lactam Hydrolysis" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of RENAL DIPEPTIDASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A RENAL DIPEPTIDASE P16444 (17-385) (DPEP1_HUMAN)search Homo sapienssearch 93% 369 100%
B RENAL DIPEPTIDASE P16444 (17-385) (DPEP1_HUMAN)search Homo sapienssearch 93% 369 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P16444 (17 - 385) RENAL DIPEPTIDASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P16444) Renal dipeptidasesearch Metal-dependent hydrolasessearch PF01244: Membrane dipeptidase (Peptidase family M19)search

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A, B (P16444) antibiotic metabolic processsearch glutathione metabolic processsearch proteolysissearch cellular response to drugsearch homocysteine metabolic processsearch negative regulation of apoptotic processsearch leukotriene metabolic processsearch cellular response to nitric oxidesearch arachidonic acid metabolic processsearch cellular response to calcium ionsearch small molecule metabolic processsearch negative regulation of cell migrationsearch negative regulation of cysteine-type endopeptidase activity involved in apoptotic processsearch cellular lactam catabolic processsearch extracellular spacesearch apical part of cellsearch membranesearch plasma membranesearch cell projectionsearch anchored to membranesearch apical plasma membranesearch extracellular vesicular exosomesearch microvillus membranesearch metal ion bindingsearch dipeptidase activitysearch metalloexopeptidase activitysearch dipeptidyl-peptidase activitysearch hydrolase activitysearch GPI anchor bindingsearch cysteine-type endopeptidase inhibitor activity involved in apoptotic processsearch peptidase activitysearch protein bindingsearch metallopeptidase activitysearch metallodipeptidase activitysearch zinc ion bindingsearch modified amino acid bindingsearch

Chain InterPro annotation
A, B Renal dipeptidase, active sitesearch Renal dipeptidase familysearch