Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7Q3Y

Structure of full-length, monomeric, soluble somatic angiotensin I-converting enzyme showing the N- and C-terminal ellipsoid domains

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0001822biological_processkidney development
A0001974biological_processblood vessel remodeling
A0002003biological_processangiotensin maturation
A0002019biological_processregulation of renal output by 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
A0004222molecular_functionmetalloendopeptidase activity
A0005516molecular_functioncalmodulin binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0007283biological_processspermatogenesis
A0007565biological_processfemale pregnancy
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
A0009410biological_processresponse to xenobiotic stimulus
A0009792biological_processembryo development ending in birth or egg hatching
A0009897cellular_componentexternal side of plasma membrane
A0009925cellular_componentbasal 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
A0019229biological_processregulation of vasoconstriction
A0030324biological_processlung development
A0031100biological_processanimal organ regeneration
A0031404molecular_functionchloride ion binding
A0031434molecular_functionmitogen-activated protein kinase kinase binding
A0031526cellular_componentbrush border membrane
A0031667biological_processresponse to nutrient levels
A0031711molecular_functionbradykinin receptor binding
A0031982cellular_componentvesicle
A0032496biological_processresponse to lipopolysaccharide
A0032943biological_processmononuclear cell proliferation
A0034616biological_processresponse to laminar fluid shear stress
A0038166biological_processangiotensin-activated signaling pathway
A0042310biological_processvasoconstriction
A0042445biological_processhormone metabolic process
A0042447biological_processhormone catabolic process
A0042755biological_processeating behavior
A0043065biological_processpositive regulation of apoptotic process
A0043171biological_processpeptide catabolic process
A0045777biological_processpositive regulation of blood pressure
A0045907biological_processpositive regulation of vasoconstriction
A0046325biological_processnegative regulation of glucose import
A0046872molecular_functionmetal ion binding
A0048167biological_processregulation of synaptic plasticity
A0048286biological_processlung alveolus development
A0050435biological_processamyloid-beta metabolic process
A0050482biological_processarachidonic acid secretion
A0050769biological_processpositive regulation of neurogenesis
A0051019molecular_functionmitogen-activated protein kinase binding
A0060047biological_processheart contraction
A0060177biological_processregulation of angiotensin metabolic process
A0060218biological_processhematopoietic stem cell differentiation
A0060978biological_processangiogenesis involved in coronary vascular morphogenesis
A0070062cellular_componentextracellular exosome
A0070573molecular_functionmetallodipeptidase activity
A0071333biological_processcellular response to glucose stimulus
A0071548biological_processresponse to dexamethasone
A0071838biological_processcell proliferation in bone marrow
A0086091biological_processregulation of heart rate by cardiac conduction
A0090281biological_processnegative regulation of calcium ion import
A0097066biological_processresponse to thyroid hormone
A0097225cellular_componentsperm midpiece
A0097746biological_processblood vessel diameter maintenance
A1901363molecular_functionheterocyclic compound binding
A1902033biological_processregulation of hematopoietic stem cell proliferation
A1903597biological_processnegative regulation of gap junction assembly
A1904045biological_processcellular response to aldosterone
A2000170biological_processpositive regulation of peptidyl-cysteine S-nitrosylation
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
DetailsACT_SITE: Proton acceptor 1 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553
ChainResidueDetails
AGLU362

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor 1 => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AHIS491

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor 2 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553
ChainResidueDetails
AGLU960

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor 2 => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AHIS1089

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442
ChainResidueDetails
ATYR202
AARG500

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:2OC2, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AHIS361
AHIS365
AGLU389

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854
ChainResidueDetails
AARG762
ATYR800
ATRP1061
AARG1065

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:23056909, ECO:0007744|PDB:4APH
ChainResidueDetails
AHIS959
AHIS963

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:7961923, ECO:0007744|PDB:4APH
ChainResidueDetails
AGLU987

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:11432860
ChainResidueDetails
AARG1098

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:20826823
ChainResidueDetails
AASN494

site_idSWS_FT_FI12
Number of Residues1
DetailsSITE: Cleavage => ECO:0000269|PubMed:7499427, ECO:0000269|PubMed:8253769
ChainResidueDetails
AARG1137

site_idSWS_FT_FI13
Number of Residues1
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN1196

site_idSWS_FT_FI14
Number of Residues1
DetailsSITE: Cleavage => ECO:0000269|PubMed:10769174
ChainResidueDetails
AARG1203

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823, ECO:0000305|PubMed:9013598
ChainResidueDetails
AASN9

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN25
AASN117

site_idSWS_FT_FI17
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AASN45

site_idSWS_FT_FI18
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN82

site_idSWS_FT_FI19
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823
ChainResidueDetails
AASN131

site_idSWS_FT_FI20
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442
ChainResidueDetails
AASN289

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AASN416

site_idSWS_FT_FI22
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:26403559, ECO:0000269|PubMed:9013598, ECO:0007744|PDB:3NXQ
ChainResidueDetails
AASN480

site_idSWS_FT_FI23
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23056909, ECO:0007744|PDB:4APH
ChainResidueDetails
AASN648

site_idSWS_FT_FI24
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN666

site_idSWS_FT_FI25
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:9013598, ECO:0007744|PDB:4APH
ChainResidueDetails
AASN685

site_idSWS_FT_FI26
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:9013598
ChainResidueDetails
AASN731
AASN913
AASN1162

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

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon