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5ZKQ

Crystal structure of the human platelet-activating factor receptor in complex with ABT-491

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0004992molecular_functionplatelet activating factor receptor activity
A0006935biological_processchemotaxis
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
B0003796molecular_functionlysozyme activity
B0004930molecular_functionG protein-coupled receptor activity
B0004992molecular_functionplatelet activating factor receptor activity
B0006935biological_processchemotaxis
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 9EU A 501
ChainResidue
ATYR22
AHIS188
AILE191
AGLN252
ALEU279
AOLC502
ATRP73
ATYR77
AGLY94
APHE97
ACYS173
APHE174
AGLU175
ATYR177

site_idAC2
Number of Residues6
Detailsbinding site for residue OLC A 502
ChainResidue
ATYR151
APHE152
AGLU178
APRO183
APHE190
A9EU501

site_idAC3
Number of Residues3
Detailsbinding site for residue OLC A 503
ChainResidue
ATYR151
ALEU155
AASP156

site_idAC4
Number of Residues5
Detailsbinding site for residue OLC A 504
ChainResidue
ATYR102
AVAL143
AALA144
AILE145
ASER194

site_idAC5
Number of Residues1
Detailsbinding site for residue OLC A 505
ChainResidue
ALEU153

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN A 506
ChainResidue
AHIS4
AHIS8
AGLU259
AHIS268
AASN272

site_idAC7
Number of Residues16
Detailsbinding site for residue 9EU B 1201
ChainResidue
BTYR22
BTRP73
BTYR77
BGLY94
BPHE97
BPHE98
BPHE152
BCYS173
BPHE174
BGLU175
BTYR177
BHIS188
BILE191
BHIS248
BGLN252
BOLC1202

site_idAC8
Number of Residues5
Detailsbinding site for residue OLC B 1202
ChainResidue
BSER181
BPRO183
BVAL184
B9EU1201
BOLC1203

site_idAC9
Number of Residues2
Detailsbinding site for residue OLC B 1203
ChainResidue
BTYR151
BOLC1202

site_idAD1
Number of Residues6
Detailsbinding site for residue OLC B 1204
ChainResidue
BASN58
BMET61
BARG131
BILE135
BLEU139
BTRP142

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 1205
ChainResidue
BHIS8
BGLU259
BHIS268
BASN272

site_idAD3
Number of Residues2
Detailsbinding site for residue SO4 B 1206
ChainResidue
BMET1062
BSO41211

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 B 1207
ChainResidue
BGLY166
BARG1032
BARG1036

site_idAD5
Number of Residues2
Detailsbinding site for residue SO4 B 1208
ChainResidue
BARG1075
BARG1081

site_idAD6
Number of Residues1
Detailsbinding site for residue SO4 B 1209
ChainResidue
BGLY1069

site_idAD7
Number of Residues4
Detailsbinding site for residue SO4 B 1210
ChainResidue
BTHR1098
BPRO1099
BASN1100
BARG1101

site_idAD8
Number of Residues2
Detailsbinding site for residue SO4 B 1211
ChainResidue
BGLY1066
BSO41206

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. CSVaFLGVITYNRYQaV
ChainResidueDetails
ACYS103-VAL119

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues130
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 921
ChainResidueDetails

248636

PDB entries from 2026-02-04

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