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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5LHD

Structure of glycosylated human aminopeptidase N

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001618molecular_functionvirus receptor activity
A0002003biological_processangiotensin maturation
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005765cellular_componentlysosomal membrane
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0009897cellular_componentexternal side of plasma membrane
A0016285molecular_functionalanyl aminopeptidase activity
A0016787molecular_functionhydrolase activity
A0030154biological_processcell differentiation
A0030667cellular_componentsecretory granule membrane
A0038023molecular_functionsignaling receptor activity
A0043171biological_processpeptide catabolic process
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
A0070062cellular_componentextracellular exosome
B0001525biological_processangiogenesis
B0001618molecular_functionvirus receptor activity
B0002003biological_processangiotensin maturation
B0004177molecular_functionaminopeptidase activity
B0005615cellular_componentextracellular space
B0005765cellular_componentlysosomal membrane
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0009897cellular_componentexternal side of plasma membrane
B0016285molecular_functionalanyl aminopeptidase activity
B0016787molecular_functionhydrolase activity
B0030154biological_processcell differentiation
B0030667cellular_componentsecretory granule membrane
B0038023molecular_functionsignaling receptor activity
B0043171biological_processpeptide catabolic process
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
B0070062cellular_componentextracellular exosome
C0001525biological_processangiogenesis
C0001618molecular_functionvirus receptor activity
C0002003biological_processangiotensin maturation
C0004177molecular_functionaminopeptidase activity
C0005615cellular_componentextracellular space
C0005765cellular_componentlysosomal membrane
C0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
C0005886cellular_componentplasma membrane
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0009897cellular_componentexternal side of plasma membrane
C0016285molecular_functionalanyl aminopeptidase activity
C0016787molecular_functionhydrolase activity
C0030154biological_processcell differentiation
C0030667cellular_componentsecretory granule membrane
C0038023molecular_functionsignaling receptor activity
C0043171biological_processpeptide catabolic process
C0046718biological_processsymbiont entry into host cell
C0046872molecular_functionmetal ion binding
C0070006molecular_functionmetalloaminopeptidase activity
C0070062cellular_componentextracellular exosome
D0001525biological_processangiogenesis
D0001618molecular_functionvirus receptor activity
D0002003biological_processangiotensin maturation
D0004177molecular_functionaminopeptidase activity
D0005615cellular_componentextracellular space
D0005765cellular_componentlysosomal membrane
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005886cellular_componentplasma membrane
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0008237molecular_functionmetallopeptidase activity
D0008270molecular_functionzinc ion binding
D0009897cellular_componentexternal side of plasma membrane
D0016285molecular_functionalanyl aminopeptidase activity
D0016787molecular_functionhydrolase activity
D0030154biological_processcell differentiation
D0030667cellular_componentsecretory granule membrane
D0038023molecular_functionsignaling receptor activity
D0043171biological_processpeptide catabolic process
D0046718biological_processsymbiont entry into host cell
D0046872molecular_functionmetal ion binding
D0070006molecular_functionmetalloaminopeptidase activity
D0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW
ChainResidueDetails
AVAL385-TRP394
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsRegion: {"description":"Necessary and sufficient to mediate interaction with HCoV-229E","evidences":[{"source":"PubMed","id":"1350662","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8887485","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"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FYQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FYR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FYT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues16
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22932899","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2694
DetailsRegion: {"description":"Metalloprotease"}
ChainResidueDetails

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PDB entries from 2025-12-03

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