2iul Summary



The structure was published by Watermeyer, J.M., Sewell, B.T., Schwager, S.L., et al., Corradi, H.R., Acharya, K.R., and Sturrock, E.D., in 2006 in a paper entitled "Structure of Testis Ace Glycosylation Mutants and Evidence for Conserved Domain Movement." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2006.

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

The PDB entry contains the structure of ANGIOTENSIN-CONVERTING ENZYME. 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 582 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 P12821 (642-1232) (ACE_HUMAN)search Homo sapienssearch < 90% 591 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12821 (642 - 1232) ANGIOTENSIN-CONVERTING ENZYME Homo sapiens

Chain Sequence family (Pfam)
A Angiotensin-converting enzymesearch

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

Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch