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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
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
B0003796molecular_functionlysozyme activity
B0004930molecular_functionG protein-coupled receptor activity
B0004992molecular_functionplatelet activating factor receptor activity
B0006935biological_processchemotaxis
B0007186biological_processG protein-coupled receptor signaling pathway
B0009253biological_processpeptidoglycan catabolic process
B0016020cellular_componentmembrane
B0016998biological_processcell wall macromolecule catabolic process
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
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
ALEU17-TRP38
BLEU17-TRP38

site_idSWS_FT_FI2
Number of Residues68
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AVAL39-ILE54
AASN114-ARG133
BVAL39-ILE54
BASN114-ARG133

site_idSWS_FT_FI3
Number of Residues38
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
APHE55-ILE74
BPHE55-ILE74

site_idSWS_FT_FI4
Number of Residues130
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AVAL75-ASN91
AASP156-VAL184
ATRP255-GLN276
BVAL75-ASN91
BASP156-VAL184
BTRP255-GLN276

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AVAL92-TYR113
BVAL92-TYR113

site_idSWS_FT_FI6
Number of Residues42
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AGLY134-LEU155
BGLY134-LEU155

site_idSWS_FT_FI7
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
ALEU185-CYS205
BLEU185-CYS205

site_idSWS_FT_FI8
Number of Residues40
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AALA234-PRO254
BALA234-PRO254

site_idSWS_FT_FI9
Number of Residues38
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
AVAL277-LEU296
BVAL277-LEU296

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASP169
BASP169

site_idSWS_FT_FI11
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1010
BGLU1010

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
APHE1060
BPHE1060

site_idSWS_FT_FI13
Number of Residues4
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1073
AASN1088
BSER1073
BASN1088

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 921
ChainResidueDetails
AGLU1010proton shuttle (general acid/base)

site_idMCSA2
Number of Residues1
DetailsM-CSA 921
ChainResidueDetails
BGLU1010proton shuttle (general acid/base)

218853

數據於2024-04-24公開中

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