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4F5C

Crystal structure of the spike receptor binding domain of a porcine respiratory coronavirus in complex with the pig aminopeptidase N ectodomain

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001618molecular_functionvirus receptor activity
A0002003biological_processangiotensin maturation
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016285molecular_functionalanyl aminopeptidase activity
A0016787molecular_functionhydrolase activity
A0030154biological_processcell differentiation
A0043171biological_processpeptide catabolic process
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0001525biological_processangiogenesis
B0001618molecular_functionvirus receptor activity
B0002003biological_processangiotensin maturation
B0004177molecular_functionaminopeptidase activity
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0016285molecular_functionalanyl aminopeptidase activity
B0016787molecular_functionhydrolase activity
B0030154biological_processcell differentiation
B0043171biological_processpeptide catabolic process
B0046718biological_processsymbiont entry into host cell
B0046872molecular_functionmetal ion binding
B0070006molecular_functionmetalloaminopeptidase activity
E0019064biological_processfusion of virus membrane with host plasma membrane
F0019064biological_processfusion of virus membrane with host plasma membrane
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 Residues192
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 Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P15144","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22876187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4F5C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P15144","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
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 Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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