4aa1 Summary

pdbe.org/4aa1
spacer

Crystal structure of ANCE in complex with Angiotensin-II

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 2011.

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 ANGIOTENSIN-2.

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 ANGIOTENSIN-2 P01019 (34-41) (ANGT_HUMAN)search Homo sapienssearch 100% 8 62%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q10714 (17 - 614) ANGIOTENSIN-CONVERTING ENZYME Drosophila melanogaster
P01019 (34 - 41) ANGIOTENSIN-2 Homo sapiens

Chain Sequence family (Pfam)
A Angiotensin-converting enzymesearch
P (P01019)

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

Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch
P