3bkk Summary


Tesis ACE co-crystal structure with ketone ACE inhibitor kAF

The structure was published by Watermeyer, J.M., Kroger, W.L., O'Neill, H.G., Sewell, B.T., and Sturrock, E.D., in 2008 in a paper entitled "Probing the basis of domain-dependent inhibition using novel ketone inhibitors of Angiotensin-converting enzyme" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.17 Å and deposited in 2007.

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

The PDB entry contains the structure of Angiotensin-converting enzyme, somatic isoform. This molecule has the UniProt identifier P12821 (ACE_HUMAN)search. The sample contained 591 residues which is < 90% of the natural sequence. Out of 591 residues 586 were observed and are deposited in the PDB.

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 is most likely monomeric.

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, somatic isoform P12821 (642-1232) (ACE_HUMAN)search Homo sapienssearch < 90% 591 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12821 (642 - 1232) Angiotensin-converting enzyme, somatic isoform Homo sapiens

Chain Sequence family (Pfam)
A Angiotensin-converting enzymesearch

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

Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch