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6AK3

Crystal structure of the human prostaglandin E receptor EP3 bound to prostaglandin E2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004955molecular_functionprostaglandin receptor activity
A0004957molecular_functionprostaglandin E receptor activity
A0005506molecular_functioniron ion binding
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
B0004930molecular_functionG protein-coupled receptor activity
B0004955molecular_functionprostaglandin receptor activity
B0004957molecular_functionprostaglandin E receptor activity
B0005506molecular_functioniron ion binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
B0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue P2E B 1201
ChainResidue
BMET58
BARG333
BSER336
BGLN339
BGLN103
BTHR106
BTHR107
BVAL110
BTYR114
BMET137
BTHR206
BTRP207

site_idAC2
Number of Residues10
Detailsbinding site for residue POV B 1202
ChainResidue
ASER49
AILE330
AARG333
ALEU341
BVAL50
BSER51
BVAL52
BALA53
BTHR57
BTYR114

site_idAC3
Number of Residues13
Detailsbinding site for residue P2E A 1201
ChainResidue
AMET58
AGLN103
ATHR106
ATHR107
AVAL110
ATYR114
AMET137
ATHR206
ATRP207
ALEU329
AARG333
ASER336
AGLN339

site_idAC4
Number of Residues10
Detailsbinding site for residue POV A 1202
ChainResidue
AVAL50
ASER51
AVAL52
AALA53
ATHR57
ALEU60
BGLY48
BSER49
BILE330
BARG333

Functional Information from PROSITE/UniProt
site_idPS00626
Number of Residues11
DetailsRCC1_2 Regulator of chromosome condensation (RCC1) signature 2. AGSGsGHGFDI
ChainResidueDetails
BALA1040-ILE1067

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
BPHE54-ARG78
APHE54-ARG78

site_idSWS_FT_FI2
Number of Residues124
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BARG79-CYS91
BGLU154-ARG175
BLYS254-GLN283
AARG79-CYS91
AGLU154-ARG175
ALYS254-GLN283

site_idSWS_FT_FI3
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
BILE92-VAL112
AILE92-VAL112

site_idSWS_FT_FI4
Number of Residues132
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BVAL113-THR131
BGLN198-ASN227
BGLN308-PHE327
AVAL113-THR131
AGLN198-ASN227
AGLN308-PHE327

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
BPHE132-VAL153
APHE132-VAL153

site_idSWS_FT_FI6
Number of Residues42
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
BALA176-GLY197
AALA176-GLY197

site_idSWS_FT_FI7
Number of Residues50
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
BLEU228-ILE253
ALEU228-ILE253

site_idSWS_FT_FI8
Number of Residues46
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
BLEU284-PHE307
ALEU284-PHE307

site_idSWS_FT_FI9
Number of Residues42
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
BPHE328-LEU349
APHE328-LEU349

site_idSWS_FT_FI10
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
BTRP1007
BILE1102
ATRP1007
AILE1102

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PDB entries from 2024-07-17

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