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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5TUD

Structural Insights into the Extracellular Recognition of the Human Serotonin 2B Receptor by an Antibody

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
A0006939biological_processsmooth muscle contraction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007507biological_processheart development
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022900biological_processelectron transport chain
A0042310biological_processvasoconstriction
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
A0050795biological_processregulation of behavior
D0004930molecular_functionG protein-coupled receptor activity
D0004993molecular_functionG protein-coupled serotonin receptor activity
D0005506molecular_functioniron ion binding
D0005886cellular_componentplasma membrane
D0006939biological_processsmooth muscle contraction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007507biological_processheart development
D0009055molecular_functionelectron transfer activity
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
D0022900biological_processelectron transport chain
D0042310biological_processvasoconstriction
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
D0050795biological_processregulation of behavior
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ERM A 2001
ChainResidue
AASP135
APHE340
APHE341
ALEU347
AGLN359
ALEU362
AGLU363
AVAL366
AVAL136
ASER139
ATHR140
AVAL208
ALEU209
ALYS211
AMET218
AALA225
site_idAC2
Number of Residues17
Detailsbinding site for residue ERM D 1201
ChainResidue
DASP135
DSER139
DTHR140
DVAL208
DLEU209
DTHR210
DMET218
DALA225
DPHE340
DPHE341
DASN344
DVAL348
DGLN359
DLEU362
DGLU363
DVAL366
DTYR370
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
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
BTYR191-HIS197
CTYR208-HIS214
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues58
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues104
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsMotif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues6
DetailsMotif: {"description":"[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues8
DetailsMotif: {"description":"NPxxY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IB4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NC3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Hydrophobic barrier that decreases the speed of ligand binding and dissociation","evidences":[{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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