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5LDS

Structure of the porcine aminopeptidase N ectodomain

Functional Information from GO Data
ChainGOidnamespacecontents
A0002003biological_processangiotensin maturation
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016285molecular_functionalanyl aminopeptidase activity
A0043171biological_processpeptide catabolic process
A0070006molecular_functionmetalloaminopeptidase activity
B0002003biological_processangiotensin maturation
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016285molecular_functionalanyl aminopeptidase activity
B0043171biological_processpeptide catabolic process
B0070006molecular_functionmetalloaminopeptidase activity
C0002003biological_processangiotensin maturation
C0005886cellular_componentplasma membrane
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0016285molecular_functionalanyl aminopeptidase activity
C0043171biological_processpeptide catabolic process
C0070006molecular_functionmetalloaminopeptidase activity
D0002003biological_processangiotensin maturation
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0016285molecular_functionalanyl aminopeptidase activity
D0043171biological_processpeptide catabolic process
D0070006molecular_functionmetalloaminopeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
AVAL380-TRP389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues384
DetailsRegion: {"description":"Interaction with TGEV spike glycoprotein","evidences":[{"source":"PubMed","id":"7913510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8985407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634079","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P15144","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22876187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F5C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P15144","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22876187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F5C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

253389

PDB entries from 2026-05-13

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