4IB4
Crystal structure of the chimeric protein of 5-HT2B-BRIL in complex with ergotamine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ERM A 2001 |
Chain | Residue |
A | ASP135 |
A | ALA225 |
A | TRP337 |
A | PHE340 |
A | ASN344 |
A | LEU347 |
A | GLN359 |
A | HOH2020 |
A | VAL136 |
A | SER139 |
A | THR140 |
A | VAL208 |
A | LEU209 |
A | THR210 |
A | LYS211 |
A | MET218 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PLM A 2002 |
Chain | Residue |
A | ILE66 |
A | THR343 |
A | ILE395 |
A | THR396 |
A | CYS397 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CLR A 2003 |
Chain | Residue |
A | GLY70 |
A | THR73 |
A | TYR394 |
A | TYR399 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE OLC A 2004 |
Chain | Residue |
A | SER150 |
A | MET233 |
A | THR240 |
A | LEU326 |
A | HOH2017 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE OLB A 2005 |
Chain | Residue |
A | PRO191 |
A | ILE192 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OLB A 2006 |
Chain | Residue |
A | MET360 |
A | TYR399 |
A | OLB2007 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE OLB A 2007 |
Chain | Residue |
A | LEU81 |
A | TYR399 |
A | OLB2006 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE OLA A 2008 |
Chain | Residue |
A | TRP56 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OLA A 2009 |
Chain | Residue |
A | GLY185 |
A | LYS193 |
A | ASP216 |
A | PHE217 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A 2010 |
Chain | Residue |
A | TYR380 |
A | ASN384 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PEG A 2011 |
Chain | Residue |
A | ILE182 |
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCAISVDRYIaI |
Chain | Residue | Details |
A | ALA141-ILE157 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Binding site: {"description":"axial binding residue"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 29 |
Details | Topological 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 22 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 29 |
Details | Topological 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 21 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 22 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | Transmembrane: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Motif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
Details | Motif: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | Motif: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IB4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NC3","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Site: {"description":"Hydrophobic barrier that decreases the speed of ligand binding and dissociation","evidences":[{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |