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6DS0

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 Residues6
Detailsbinding site for residue CLR A 1201
ChainResidue
AILE61
AILE66
AGLY70
ATHR73
ATYR394
ATYR399

site_idAC2
Number of Residues5
Detailsbinding site for residue OLC A 1202
ChainResidue
ATHR240
ALEU326
AALA58
ASER150
AMET233

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 1203
ChainResidue
ATYR380
APHE383
AASN384

site_idAC4
Number of Residues12
Detailsbinding site for residue H8M A 1204
ChainResidue
ATHR114
AASP135
AVAL136
ALEU209
APHE217
AGLY221
APHE340
AASN344
ALEU362
AGLU363
AVAL366
ATYR370

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 Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ATRP1007
AILE1102

222624

PDB entries from 2024-07-17

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