4aph Summary


Human angiotensin-converting enzyme in complex with angiotensin-II

The structure was published by Masuyer, G., Schwager, S.L.U., Sturrock, E.D., Isaac, R.E., and Acharya, K.R., in 2012 in a paper entitled "Molecular Recognition and Regulation of Human Angiotensin-I Converting Enzyme (Ace) Activity by Natural Inhibitory Peptides." (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 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 P12821 (642-1230) (ACE_HUMAN)search Homo sapienssearch < 90% 589 98%
P ANGIOTENSIN-2 P01019 (34-41) (ANGT_HUMAN)search Homo sapienssearch 100% 8 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P12821 (642 - 1230) ANGIOTENSIN-CONVERTING ENZYME Homo sapiens

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

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P12821) membranesearch proteolysissearch metallopeptidase activitysearch peptidyl-dipeptidase activitysearch

Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch