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4CA5

Human Angiotensin converting enzyme in complex with a phosphinic tripeptide FI

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
DetailsACT_SITE: Proton acceptor 1 => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:12540854, ECO:0000305|PubMed:16154999, ECO:0000305|PubMed:19773553
ChainResidueDetails
ATYR360

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 Residues
DetailsM-CSA 170
ChainResidueDetails

218853

PDB entries from 2024-04-24

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