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Protein Information: Beta-1 adrenergic receptor

Cannonical Uniprot Accesion Number: P07700

        10         20         30         40         50
MGDGWLPPDC GPHNRSGGGG ATAAPTGSRQ VSAELLSQQW EAGMSLLMAL 
        60         70         80         90        100
VVLLIVAGNV LVIAAIGRTQ RLQTLTNLFI TSLACADLVM GLLVVPFGAT 
       110        120        130        140        150
LVVRGTWLWG SFLCECWTSL DVLCVTASIE TLCVIAIDRY LAITSPFRYQ 
       160        170        180        190        200
SLMTRARAKV IICTVWAISA LVSFLPIMMH WWRDEDPQAL KCYQDPGCCD 
       210        220        230        240        250
FVTNRAYAIA SSIISFYIPL LIMIFVYLRV YREAKEQIRK IDRCEGRFYG 
       260        270        280        290        300
SQEQPQPPPL PQHQPILGNG RASKRKTSRV MAMREHKALK TLGIIMGVFT 
       310        320        330        340        350
LCWLPFFLVN IVNVFNRDLV PDWLFVFFNW LGYANSAFNP IIYCRSPDFR 
       360        370        380        390        400
KAFKRLLCFP RKADRRLHAG GQPAPLPGGF ISTLGSPEHS PGGTWSDCNG 
       410        420        430        440        450
GTRGGSESSL EERHSKTSRS ESKMEREKNI LATTRFYCTF LGNGDKAVFC 
       460        470        480     
TVLRIVKLFE DATCTCPHTH KLKMKWRFKQ HQA

Scientific name: Meleagris gallopavo


Is this protein a mutant? False


Alternative names:


  • Beta-1 adrenoceptor

  • Beta-1 adrenoreceptor

  • Beta-T


Corresponding Cannonical Protein:


Protein ID: 231

You can find this protein in the following complex structures:


Complex Structure ID: 145 Complex Structure ID: 20 Complex Structure ID: 14 Complex Structure ID: 54 Complex Structure ID: 129 Complex Structure ID: 141 Complex Structure ID: 139 Complex Structure ID: 133 Complex Structure ID: 136 Complex Structure ID: 10 Complex Structure ID: 24 Complex Structure ID: 26 Complex Structure ID: 16 Complex Structure ID: 131 Complex Structure ID: 147 Complex Structure ID: 53 Complex Structure ID: 167 Complex Structure ID: 12 Complex Structure ID: 22

References in which this protein is mentioned:


Ismael Rodríguez-Espigares, Mariona Torrens-Fontanals, et al.. 2020. GPCRmd uncovers the dynamics of the 3D-GPCRome. Nature methods 17 (8). doi: 10.1038/s41592-020-0884-y. Available in: Pubmed Link

SUPPORTED BY

ERNEST (COST Action CA18133)

GLISTEN (COST Action CM1207)

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