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

Chain InterPro annotation
A, B Membrane dipeptidase, active sitesearch Renal dipeptidase familysearch Dipeptidase 1search