Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7Q49

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001822	biological_process	kidney development
A	0001974	biological_process	blood vessel remodeling
A	0002003	biological_process	angiotensin maturation
A	0002019	biological_process	regulation of renal output by angiotensin
A	0002446	biological_process	neutrophil mediated immunity
A	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
A	0003081	biological_process	regulation of systemic arterial blood pressure by renin-angiotensin
A	0003084	biological_process	positive regulation of systemic arterial blood pressure
A	0004175	molecular_function	endopeptidase activity
A	0004180	molecular_function	carboxypeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0005516	molecular_function	calmodulin binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005768	cellular_component	endosome
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0007283	biological_process	spermatogenesis
A	0008217	biological_process	regulation of blood pressure
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008238	molecular_function	exopeptidase activity
A	0008240	molecular_function	tripeptidyl-peptidase activity
A	0008241	molecular_function	peptidyl-dipeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0008584	biological_process	male gonad development
A	0009897	cellular_component	external side of plasma membrane
A	0010608	biological_process	post-transcriptional regulation of gene expression
A	0010629	biological_process	negative regulation of gene expression
A	0010814	biological_process	substance P catabolic process
A	0010815	biological_process	bradykinin catabolic process
A	0014910	biological_process	regulation of smooth muscle cell migration
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019229	biological_process	regulation of vasoconstriction
A	0031404	molecular_function	chloride ion binding
A	0031434	molecular_function	mitogen-activated protein kinase kinase binding
A	0031711	molecular_function	bradykinin receptor binding
A	0032943	biological_process	mononuclear cell proliferation
A	0038166	biological_process	angiotensin-activated signaling pathway
A	0042445	biological_process	hormone metabolic process
A	0042447	biological_process	hormone catabolic process
A	0043171	biological_process	peptide catabolic process
A	0046872	molecular_function	metal ion binding
A	0048167	biological_process	regulation of synaptic plasticity
A	0050435	biological_process	amyloid-beta metabolic process
A	0050482	biological_process	arachidonate secretion
A	0051019	molecular_function	mitogen-activated protein kinase binding
A	0060047	biological_process	heart contraction
A	0060177	biological_process	regulation of angiotensin metabolic process
A	0060218	biological_process	hematopoietic stem cell differentiation
A	0070062	cellular_component	extracellular exosome
A	0070573	molecular_function	metallodipeptidase activity
A	0071838	biological_process	cell proliferation in bone marrow
A	0086091	biological_process	regulation of heart rate by cardiac conduction
A	0097746	biological_process	blood vessel diameter maintenance
A	1902033	biological_process	regulation of hematopoietic stem cell proliferation
A	1903597	biological_process	negative regulation of gap junction assembly

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVHHEMGHIQ

Chain	Residue	Details
A	THR358-GLN367
A	VAL956-GLN965

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	584
Details	Domain: {"description":"Peptidase M2 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton acceptor 1","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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26403559","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OC2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24297181","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C2N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4C2P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4C2Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4C2R","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26403559","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26403559","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16476442","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20826823","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26403559","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21810173","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24297181","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8626443","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C2O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8626443","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues
Details	M-CSA 170

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)