1o86 Summary


Crystal Structure of Human Angiotensin Converting Enzyme in complex with lisinopril.

The structure was published by Natesh, R., Schwager, S.L.U., Sturrock, E.D., and Acharya, K.R., in 2003 in a paper entitled "Crystal Structure of the Human Angiotensin-Converting Enzyme-Lisinopril Complex" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2002.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of ANGIOTENSIN CONVERTING ENZYME. This molecule has the UniProt identifier P12821 (ACE_HUMAN)search. The sample contained 589 residues which is < 90% of the natural sequence. Out of 589 residues 571 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 (642-1230) (ACE_HUMAN)search Homo sapienssearch < 90% 589 97%

This entry contains 1 unique UniProt protein:

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

Chain Structural classification (SCOP) Sequence family (Pfam)
A Neurolysin-likesearch Angiotensin-converting enzymesearch
Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch