7Z70

Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with fosinoprilat

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008241	molecular_function	peptidyl-dipeptidase activity
A	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL380-GLN389

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active 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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding 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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01355","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12540854","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11432860","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Cleavage","evidences":[{"source":"PubMed","id":"7499427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8253769","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23056909","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI11
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"9013598","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 170

Chain	Residue	Details
A	HIS353	electrostatic stabiliser, hydrogen bond acceptor
A	ALA354	electrostatic stabiliser, hydrogen bond acceptor
A	HIS383	metal ligand
A	GLU384	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS387	metal ligand
A	GLU411	metal ligand
A	SER517	electrostatic stabiliser, hydrogen bond donor
A	PHE527	electrostatic stabiliser, hydrogen bond donor

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