1pfq Summary


crystal structure of human apo dipeptidyl peptidase IV / CD26

The structure was published by Oefner, C., D'Arcy, A., Mac Sweeney, A., Pierau, S., Gardiner, R., and Dale, G.E., in 2003 in a paper entitled "High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2003.

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

This PDB entry contains multiple copies of the structure of Dipeptidyl peptidase IV soluble form.

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 Dipeptidyl peptidase IV soluble form P27487 (36-766) (DPP4_HUMAN)search Homo sapienssearch 95% 731 99%
B Dipeptidyl peptidase IV soluble form P27487 (36-766) (DPP4_HUMAN)search Homo sapienssearch 95% 731 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P27487 (36 - 766) Dipeptidyl peptidase IV soluble form Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P27487) DPP6 N-terminal domain-likesearch, DPP6 catalytic domain-likesearch Methanol Dehydrogenase; Chain Asearch, Rossmann foldsearch PF00326: Prolyl oligopeptidase familysearch, PF00930: Dipeptidyl peptidase IV (DPP IV) N-terminal regionsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B (P27487) extracellular vesicular exosomesearch membranesearch focal adhesionsearch plasma membranesearch cell surfacesearch lamellipodium membranesearch cell junctionsearch intercellular canaliculussearch invadopodium membranesearch apical plasma membranesearch extracellular regionsearch lamellipodiumsearch cell projectionsearch endocytic vesiclesearch lysosomal membranesearch integral component of membranesearch membrane raftsearch dipeptidyl-peptidase activitysearch protein bindingsearch serine-type peptidase activitysearch serine-type endopeptidase activitysearch receptor bindingsearch aminopeptidase activitysearch protein homodimerization activitysearch hydrolase activitysearch identical protein bindingsearch protease bindingsearch peptidase activitysearch cell adhesionsearch proteolysissearch regulation of cell-cell adhesion mediated by integrinsearch endothelial cell migrationsearch positive regulation of cell proliferationsearch T cell costimulationsearch negative regulation of extracellular matrix disassemblysearch response to hypoxiasearch T cell activationsearch

Chain InterPro annotation
A, B Peptidase S9, prolyl oligopeptidase, catalytic domainsearch Peptidase S9B, dipeptidylpeptidase IV N-terminalsearch Peptidase S9, serine active sitesearch Alpha/Beta hydrolase foldsearch