4asq Summary


Crystal structure of ANCE in complex with Bradykinin

The structure was published by Akif, M., Masuyer, G., Bingham, R.J., Sturrock, E.D., Isaac, R.E., and Acharya, K.R., in 2012 in a paper entitled "Structural Basis of Peptide Recognition by the Angiotensin-I Converting Enzyme Homologue Ance from Drosophila Melanogaster" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.99 Å and deposited in 2012.

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

This PDB entry contains a complex of 2 biomacromolecules, namely ANGIOTENSIN-CONVERTING ENZYME and BRADYKININ.

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 heterodimers.

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 ANGIOTENSIN-CONVERTING ENZYME Q10714 (17-614) (ACE_DROME)search Drosophila melanogastersearch < 90% 598 100%
P BRADYKININ P01042 (381-389) (KNG1_HUMAN)search Homo sapienssearch < 90% 9 44%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q10714 (17 - 614) ANGIOTENSIN-CONVERTING ENZYME Drosophila melanogaster

Chain Sequence family (Pfam)
A Angiotensin-converting enzymesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (Q10714) proteolysissearch metallopeptidase activitysearch peptidyl-dipeptidase activitysearch membranesearch

Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch