8JPD: Beta-adrenergic receptor kinase 1

Focused refinement structure of GRK2 in NTSR1-GRK2-Galpha(q) complexes. Determined by electron microscopy at 2.81 Å resolution. Released 9 Aug 2023.

Method
Electron microscopy
Resolution
2.81 Å
Organism
Bos taurus
Chains
1
Atoms
5,198
Mol. weight
80.11 kDa
Ligands
STU
Released
9 Aug 2023

Explore 8JPD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8JPD contains 39 α-helices and 19 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain G: 39 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix4-1815
α-helix24-274
α-helix34-363
α-helix37-393
α-helix40-489
α-helix55-595
α-helix62-7514
α-helix80-9314
α-helix98-10912
α-helix110-1145
α-helix115-1195
α-helix126-13712
α-helix147-15610
α-helix157-1615
α-helix162-1676
α-helix170-18213
α-helix188-1903
β-strand191-200101
β-strand203-21081
β-strand216-22381
α-helix224-2296
α-helix233-24715
β-strand25412
β-strand257-26261
β-strand266-27271
β-strand27812
α-helix279-2868
α-helix291-31020
β-strand313-31423
α-helix320-3223
β-strand323-32532
β-strand331-33332
β-strand340-34123
α-helix359-3624
α-helix371-38616
α-helix399-4024
α-helix403-4075
α-helix419-42810
α-helix444-4485
α-helix451-4533
α-helix458-4636
α-helix467-4682
α-helix482-4854
α-helix490-4934
α-helix500-5034
α-helix504-5063
β-strand511-51221
α-helix514-52411
α-helix526-54722
β-strand561-56774
β-strand577-58374
β-strand587-59154
β-strand597-60264
α-helix603-6053
β-strand606-61494
β-strand617-62484
β-strand629-63354
α-helix637-65822

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Beta-adrenergic receptor kinase 1Gprotein688Bos taurusP21146 (AlphaFold model)
Sequence of entity 1 (G), FASTA
>8JPD_1 Beta-adrenergic receptor kinase 1 (chains G)
ADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQ
KLGYLLFRDFCLKHLEEAKPLVEFYEEIKKYEKLETEEERLVCSREIFDTYIMKELLACS
HPFSKSAIEHVQGHLVKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVE
LNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERI
MLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEPDMIFYAAEI
ILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEV
LQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPEL
RSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRDLDWQMVFLQKYPPPLIPPRGEVNAAD
AFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKK
TKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSLL
TMEEIQSVEETQIKERKCLLLKIRGGKQFVLQCDSDPELVQWKKELRDAYREAQQLVQRV
PKMKNKPRSPVVELSKVPLIQRGSANGL

Ligands and cofactors

IDNameFormulaCopies
STUStaurosporineC28 H26 N4 O31

Primary citation

GPCR activation and GRK2 assembly by a biased intracellular agonist. Duan, J., Liu, H., Zhao, F. et al. Nature (2023) 620:676-681. DOI 10.1038/s41586-023-06395-9 · PubMed

Other PDB entries of the same protein (UniProt P21146 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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