3nxq Summary


Angiotensin Converting Enzyme N domain glycsoylation mutant (Ndom389) in complex with RXP407

The structure was published by Anthony, C.S., Corradi, H.R., Schwager, S.L., et al., Dive, V., Acharya, K.R., and Sturrock, E.D., in 2010 in a paper entitled "The N domain of human angiotensin-I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain-specific phosphinic inhibitor, RXP407." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.99 Å and deposited in 2010.

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.

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 P12821 (30-658) (ACE_HUMAN)search Homo sapienssearch < 90% 629 96%
B Angiotensin-converting enzyme P12821 (30-658) (ACE_HUMAN)search Homo sapienssearch < 90% 629 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12821 (30 - 658) Angiotensin-converting enzyme Homo sapiens

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

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

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