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5ZKP

Crystal structure of the human platelet-activating factor receptor in complex with SR 27417

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004992molecular_functionplatelet activating factor receptor activity
A0006935biological_processchemotaxis
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 9ER A 1201
ChainResidue
ATYR22
ATRP255
AHIS275
ALEU279
ATRP73
ATYR77
AGLY94
APHE97
APHE98
ATYR102
APHE174
AILE191

site_idAC2
Number of Residues19
Detailsbinding site for residue FMN A 1202
ChainResidue
AGLU51
ASER1009
ATHR1010
ATHR1011
AGLY1012
AASN1013
ATHR1014
ASER1057
ATHR1058
ATRP1059
AGLY1060
ACYS1092
AGLY1093
AASP1094
ATRP1097
ATYR1099
APHE1100
ACYS1101
AGLY1127

Functional Information from PROSITE/UniProt
site_idPS00201
Number of Residues17
DetailsFLAVODOXIN Flavodoxin signature. IVYgSTtGnTEytAEtI
ChainResidueDetails
AILE1005-ILE1021

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 Residues141
DetailsDomain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues15
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues65
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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