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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Q4C

Local refinement structure of the C-domain of full-length, monomeric, soluble somatic angiotensin I-converting enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0001974biological_processblood vessel remodeling
A0002003biological_processangiotensin maturation
A0002019biological_processregulation of renal output by angiotensin
A0002034biological_processmaintenance of blood vessel diameter homeostasis by renin-angiotensin
A0002446biological_processneutrophil mediated immunity
A0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
A0003081biological_processregulation of systemic arterial blood pressure by renin-angiotensin
A0003084biological_processpositive regulation of systemic arterial blood pressure
A0004175molecular_functionendopeptidase activity
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0004222molecular_functionmetalloendopeptidase activity
A0005516molecular_functioncalmodulin binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0007283biological_processspermatogenesis
A0008217biological_processregulation of blood pressure
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008238molecular_functionexopeptidase activity
A0008240molecular_functiontripeptidyl-peptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0008270molecular_functionzinc ion binding
A0008584biological_processmale gonad development
A0009897cellular_componentexternal side of plasma membrane
A0010608biological_processpost-transcriptional regulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0010814biological_processsubstance P catabolic process
A0010815biological_processbradykinin catabolic process
A0014910biological_processregulation of smooth muscle cell migration
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019229biological_processregulation of vasoconstriction
A0031404molecular_functionchloride ion binding
A0031434molecular_functionmitogen-activated protein kinase kinase binding
A0031711molecular_functionbradykinin receptor binding
A0032943biological_processmononuclear cell proliferation
A0038166biological_processangiotensin-activated signaling pathway
A0042311biological_processvasodilation
A0042445biological_processhormone metabolic process
A0042447biological_processhormone catabolic process
A0043171biological_processpeptide catabolic process
A0046872molecular_functionmetal ion binding
A0048167biological_processregulation of synaptic plasticity
A0050435biological_processamyloid-beta metabolic process
A0050482biological_processarachidonate secretion
A0051019molecular_functionmitogen-activated protein kinase binding
A0060047biological_processheart contraction
A0060177biological_processregulation of angiotensin metabolic process
A0060218biological_processhematopoietic stem cell differentiation
A0070062cellular_componentextracellular exosome
A0070573molecular_functionmetallodipeptidase activity
A0071838biological_processcell proliferation in bone marrow
A0086091biological_processregulation of heart rate by cardiac conduction
A0097746biological_processblood vessel diameter maintenance
A1902033biological_processregulation of hematopoietic stem cell proliferation
A1903597biological_processnegative regulation of gap junction assembly
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVHHEMGHIQ
ChainResidueDetails
ATHR358-GLN367
AVAL956-GLN965
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16154999","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19773553","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7961923","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11432860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Cleavage","evidences":[{"source":"PubMed","id":"7499427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8253769","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 170
ChainResidueDetails
AHIS929electrostatic stabiliser, hydrogen bond acceptor
AALA930electrostatic stabiliser, hydrogen bond acceptor
AHIS959metal ligand
AGLU960electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS963metal ligand
AGLU987metal ligand
AHIS1089electrostatic stabiliser, hydrogen bond donor
ATYR1099electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-08-06

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