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6DRY

Structural Determinants of Activation and Biased Agonism at the 5-HT2B Receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004993molecular_functionG protein-coupled serotonin receptor activity
A0005506molecular_functioniron ion binding
A0005886cellular_componentplasma membrane
A0007186biological_processG protein-coupled receptor signaling pathway
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue H8D A 2001
ChainResidue
AASP135
ATHR140
AVAL208
ALEU209
APHE217
AGLY221
AALA225
APHE340
ALEU362

site_idAC2
Number of Residues4
Detailsbinding site for residue CLR A 2002
ChainResidue
AILE61
AGLY70
ATYR394
ATYR399

site_idAC3
Number of Residues4
Detailsbinding site for residue OLA A 2003
ChainResidue
AGLY185
ALYS193
AASP216
APHE217

site_idAC4
Number of Residues8
Detailsbinding site for residue OLC A 2004
ChainResidue
AHIS55
AALA58
ASER150
AMET233
ATYR237
ATHR240
ASER323
ALEU326

site_idAC5
Number of Residues1
Detailsbinding site for residue PEG A 2005
ChainResidue
ATYR380

site_idAC6
Number of Residues7
Detailsbinding site for residue PO4 A 2006
ChainResidue
AGLN1041
ALYS1047
AASP1060
AARG1062
AHIS1063
AHIS1063
AASP1066

site_idAC7
Number of Residues2
Detailsbinding site for residue PO4 A 2007
ChainResidue
AARG388
AGLY392

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCAISVDRYIaI
ChainResidueDetails
AALA141-ILE157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
AALA57-VAL79

site_idSWS_FT_FI2
Number of Residues29
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
ASER80-ASN90
AASP152-THR171

site_idSWS_FT_FI3
Number of Residues22
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
ATYR91-LEU113

site_idSWS_FT_FI4
Number of Residues52
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
ATHR114-PRO129
ALYS193-ASP216
ATHR346-MET360

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
AALA130-VAL151

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
AALA172-ILE192

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
APHE217-LEU239

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
AVAL325-ILE345

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
ALEU361-LEU382

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23519215, ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3
ChainResidueDetails
AASP135
ATHR140
ALEU209

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538
ChainResidueDetails
ALEU209

site_idSWS_FT_FI12
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
ACYS397

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007

219140

PDB entries from 2024-05-01

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