Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5V54

Crystal structure of 5-HT1B receptor in complex with methiothepin

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
B0004930molecular_functionG protein-coupled receptor activity
B0004993molecular_functionG protein-coupled serotonin receptor activity
B0005506molecular_functioniron ion binding
B0005886cellular_componentplasma membrane
B0007186biological_processG protein-coupled receptor signaling pathway
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0022900biological_processelectron transport chain
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 89F A 1201
ChainResidue
ATRP125
ATRP327
APHE330
APHE331
ATHR355
ATYR359
ALEU126
AASP129
AILE130
ACYS133
ATHR134
AILE137
AVAL201
ATHR213

site_idAC2
Number of Residues12
Detailsbinding site for residue 89F B 1201
ChainResidue
BASP129
BILE130
BCYS133
BTHR134
BILE137
BTHR213
BTRP327
BPHE330
BPHE331
BSER334
BTHR355
BTYR359

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCVIALDRYWaI
ChainResidueDetails
AALA135-ILE151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues64
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues34
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29925951","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6G79","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsMotif: {"description":"DRY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsMotif: {"description":"NPxxY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23519210","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IAR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsSite: {"description":"Important for species-specific agonist sensitivity","evidences":[{"source":"PubMed","id":"23519210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

PDB statisticsPDBj update infoContact PDBjnumon