1uze Summary

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COMPLEX OF THE ANTI-HYPERTENSIVE DRUG ENALAPRILAT AND THE HUMAN TESTICULAR ANGIOTENSIN I-CONVERTING ENZYME

The structure was published by Natesh, R., Schwager, S.L.U., Evans, H.R., Sturrock, E.D., and Acharya, K.R., in 2004 in a paper entitled "Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.82 Å and deposited in 2004.

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

Chain InterPro annotation
A Peptidase M2, peptidyl-dipeptidase Asearch