2c6f Summary

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STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN

The structure was published by Corradi, H.R., Schwager, S.L.U., Nchinda, A.T., Sturrock, E.D., and Acharya, K.R., in 2006 in a paper entitled "Crystal Structure of the N Domain of Human Somatic Angiotensin I-Converting Enzyme Provides a Structural Basis for Domain-Specific Inhibitor Design." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.01 Å and deposited in 2005.

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

This PDB entry contains multiple copies of the structure of ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 (30-641) (ACE_HUMAN)search Homo sapienssearch < 90% 612 100%
B ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM P12821 (30-641) (ACE_HUMAN)search Homo sapienssearch < 90% 612 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12821 (30 - 641) ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM Homo sapiens

Chain Sequence family (Pfam)
A, B Angiotensin-converting enzymesearch

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

Chain InterPro annotation
A, B Peptidase M2, peptidyl-dipeptidase Asearch