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4XNV

The human P2Y1 receptor in complex with BPTU

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0005506molecular_functioniron ion binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0030168biological_processplatelet activation
A0043448biological_processalkane catabolic process
A0045028molecular_functionG protein-coupled purinergic nucleotide receptor activity
A0046872molecular_functionmetal ion binding
A0090075biological_processrelaxation of muscle
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue BUR A 1101
ChainResidue
APHE62
AOLC1107
AOLC1110
AOLC1113
A1PE1114
APHE66
ALEU102
ATHR103
APRO105
AALA106
AMET123
AGLN127
AY011105

site_idAC2
Number of Residues5
Detailsbinding site for residue CLR A 1102
ChainResidue
APRO185
ATYR189
ASER213
ATYR217
AY011103

site_idAC3
Number of Residues8
Detailsbinding site for residue Y01 A 1103
ChainResidue
AILE216
ACYS220
AALA270
AMET279
AARG301
ATHR305
ACLR1102
A1PE1114

site_idAC4
Number of Residues7
Detailsbinding site for residue Y01 A 1104
ChainResidue
ATYR89
ACYS144
AHIS148
AALA224
ALEU232
ATYR246
ALEU266

site_idAC5
Number of Residues9
Detailsbinding site for residue Y01 A 1105
ChainResidue
APHE62
AILE108
APHE109
APHE112
AASN113
AARG301
ABUR1101
AOLC1113
A1PE1114

site_idAC6
Number of Residues5
Detailsbinding site for residue OLC A 1106
ChainResidue
AARG212
APHE215
AILE216
AASP289
AOLC1112

site_idAC7
Number of Residues9
Detailsbinding site for residue OLC A 1107
ChainResidue
APHE109
ASER184
APHE188
ATYR189
ATYR210
ASER213
AARG301
ABUR1101
A1PE1114

site_idAC8
Number of Residues4
Detailsbinding site for residue OLC A 1108
ChainResidue
AASP121
APHE129
AOLC1110
AHOH1206

site_idAC9
Number of Residues6
Detailsbinding site for residue OLC A 1109
ChainResidue
ALYS46
APHE49
ATYR53
APHE112
ACYS318
AOLC1111

site_idAD1
Number of Residues10
Detailsbinding site for residue OLC A 1110
ChainResidue
AILE118
APHE119
AASP121
AMET123
ALYS125
ASER184
ALEU187
APHE188
ABUR1101
AOLC1108

site_idAD2
Number of Residues6
Detailsbinding site for residue OLC A 1111
ChainResidue
APHE51
ATYR52
APRO55
ATYR111
APHE112
AOLC1109

site_idAD3
Number of Residues5
Detailsbinding site for residue OLC A 1112
ChainResidue
APHE226
ATHR281
AMET282
AARG285
AOLC1106

site_idAD4
Number of Residues9
Detailsbinding site for residue OLC A 1113
ChainResidue
ATHR267
AALA270
AARG301
ATHR305
AVAL308
ABUR1101
AY011105
A1PE1114
AHOH1217

site_idAD5
Number of Residues6
Detailsbinding site for residue 1PE A 1114
ChainResidue
AY011105
AOLC1107
AOLC1113
AARG301
ABUR1101
AY011103

site_idAD6
Number of Residues4
Detailsbinding site for residue ZN A 1115
ChainResidue
ACYS1006
ACYS1009
ACYS1039
ACYS1042

Functional Information from PROSITE/UniProt
site_idPS00202
Number of Residues11
DetailsRUBREDOXIN Rubredoxin signature. IpDDWvCPlCG
ChainResidueDetails
AILE1033-GLY1043

site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. GSIlFLTCISAHRYSgV
ChainResidueDetails
AGLY137-VAL153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues58
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4XNW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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