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):
This entry contains 2 unique UniProt proteins: