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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
A0004177molecular_functionaminopeptidase activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0030154biological_processcell differentiation
A0042277molecular_functionpeptide binding
A0043171biological_processpeptide catabolic process
A0046718biological_processsymbiont entry into host cell
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
B0001525biological_processangiogenesis
B0001618molecular_functionvirus receptor activity
B0004177molecular_functionaminopeptidase activity
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0030154biological_processcell differentiation
B0042277molecular_functionpeptide binding
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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU384
BGLU384

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P15144
ChainResidueDetails
AGLY347
BGLY347

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22876187, ECO:0007744|PDB:4F5C
ChainResidueDetails
AHIS383
AHIS387
AGLU406
BHIS383
BHIS387
BGLU406

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P15144
ChainResidueDetails
ATYR472
BTYR472

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
ATYR171
BTYR171

site_idSWS_FT_FI6
Number of Residues20
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22876187, ECO:0007744|PDB:4F5C
ChainResidueDetails
AASN82
AASN736
BASN82
BASN124
BASN229
BASN237
BASN314
BASN328
BASN506
BASN622
BASN646
AASN124
BASN736
AASN229
AASN237
AASN314
AASN328
AASN506
AASN622
AASN646

site_idSWS_FT_FI7
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN258
AASN286
AASN556
AASN569
BASN258
BASN286
BASN556
BASN569

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PDB entries from 2024-07-10

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