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4APH

Human angiotensin-converting enzyme in complex with angiotensin-II

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008241molecular_functionpeptidyl-dipeptidase activity
A0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAHHEMGHIQ
ChainResidueDetails
AVAL380-GLN389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3934016
ChainResidueDetails
PILE5

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor 1 => ECO:0000255|PROSITE-ProRule:PRU01355
ChainResidueDetails
AARG489

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:16476442
ChainResidueDetails
ATYR200
APRO498

site_idSWS_FT_FI4
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
APHE359
ALYS363
AHIS387

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:20826823
ChainResidueDetails
ATYR492

site_idSWS_FT_FI6
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
AGLU43

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AILE80

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:9013598
ChainResidueDetails
AILE115

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20826823
ChainResidueDetails
AALA129

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16476442
ChainResidueDetails
ATYR287

site_idSWS_FT_FI11
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
AGLY414

site_idSWS_FT_FI12
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
ALYS478

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 170
ChainResidueDetails
AHIS353electrostatic stabiliser, hydrogen bond acceptor
AALA354electrostatic stabiliser, hydrogen bond acceptor
AHIS383metal ligand
AGLU384electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS387metal ligand
AGLU411metal ligand
AHIS513electrostatic stabiliser, hydrogen bond donor
ATYR523electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-06-11

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