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4PXZ

Crystal structure of P2Y12 receptor in complex with 2MeSADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0005506molecular_functioniron ion binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0007194biological_processnegative regulation of adenylate cyclase activity
A0007596biological_processblood coagulation
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0045028molecular_functionG protein-coupled purinergic nucleotide receptor activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 6AD A 1201
ChainResidue
AARG93
ALYS179
AHIS187
AVAL190
AASN191
ACYS194
AARG256
ATYR259
AGLN263
ALYS280
AHOH1319
ACYS97
AHOH1322
AHOH1331
AHOH1336
AHOH1348
ASER101
AVAL102
ATYR105
ASER156
AASN159
ALYS174
ACYS175

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CLR A 1202
ChainResidue
ASER55
AILE61
ALYS64
AASN65
AILE68
ATRP149
APHE153
APHE153

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC A 1203
ChainResidue
AGLN98
AILE161
AASN164

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 1204
ChainResidue
AARG231
AVAL236
ATHR275
ATYR278
ASER282
AOLC1205

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLC A 1205
ChainResidue
AASP20
AILE23
ALEU27
ASER282
AOLC1204

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 1206
ChainResidue
AASN1022
AGLN1025
AGLN1041
AARG1062
AHOH1315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues54
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues17
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9EPX4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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