3PVU: Bovine GRK2

Bovine GRK2 in complex with Gbetagamma subunits and a selective kinase inhibitor (CMPD101). Determined by X-ray diffraction at 2.48 Å resolution. Released 1 Jun 2011.

Method: X-ray diffraction
Resolution: 2.48 Å
Organism: Bos taurus
Chains: 3
Atoms: 8,132
Mol. weight: 126.87 kDa
Ligands: QRW
Released: 1 Jun 2011

Explore 3PVU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PVU contains 41 α-helices and 47 β-strands across 3 chains. 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 A: 32 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	34-36	3
α-helix	39-48	10
α-helix	55-59	5
α-helix	62-75	14
α-helix	80-93	14
α-helix	98-108	11
α-helix	109-115	7
α-helix	116-118	3
α-helix	126-137	12
α-helix	147-158	12
α-helix	160-167	8
α-helix	169-182	14
β-strand	191-199	9	1
β-strand	203-210	8	1
β-strand	216-223	8	1
α-helix	224-230	7
α-helix	233-244	12
β-strand	254	1	2
β-strand	257-262	6	1
β-strand	266-272	7	1
β-strand	278	1	2
α-helix	279-286	8
α-helix	289-290	2
α-helix	291-310	20
β-strand	313-314	2	3
α-helix	320-322	3
β-strand	323-325	3	2
β-strand	331-333	3	2
β-strand	340-341	2	3
α-helix	354-356	3
α-helix	359-362	4
α-helix	371-386	16
α-helix	399-406	8
α-helix	410-412	3
α-helix	419-428	10
α-helix	444-448	5
α-helix	451-453	3
α-helix	458-462	5
α-helix	467-468	2
α-helix	502-504	3
β-strand	511-512	2	1
α-helix	514-522	9
α-helix	526-546	21
β-strand	561-567	7	4
β-strand	577-584	8	4
β-strand	587-591	5	4
β-strand	599-602	4	4
β-strand	606-614	9	4
β-strand	617-624	8	4
β-strand	629-633	5	4
α-helix	637-660	24

Chain B: 4 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	4-25	22
α-helix	30-33	4
α-helix	38-39	2
β-strand	47-51	5	5
β-strand	58-63	6	6
β-strand	69-74	6	6
β-strand	78-83	6	6
β-strand	89-94	6	6
β-strand	100-105	6	7
β-strand	111-116	6	7
β-strand	120-125	6	7
β-strand	134-140	7	7
β-strand	146-153	8	8
β-strand	156-161	6	8
β-strand	166-170	5	8
β-strand	175-180	6	8
β-strand	187-192	6	9
β-strand	198-203	6	9
β-strand	208-212	5	9
β-strand	218-222	5	9
β-strand	229-234	6	10
β-strand	240-245	6	10
β-strand	250-254	5	10
β-strand	259-264	6	10
α-helix	272	1
β-strand	273-278	6	11
β-strand	284-289	6	11
β-strand	294-298	5	11
β-strand	304-308	5	11
β-strand	315-320	6	5
β-strand	327-331	5	5
β-strand	336-339	4	5

Chain G: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	30-44	15
α-helix	45-47	3
α-helix	53-55	3
α-helix	56-58	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-adrenergic receptor kinase 1	A	protein	695	Bos taurus	P21146 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1	B	protein	340	Bos taurus	P62871 (AlphaFold model)
Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2	G	protein	74	Bos taurus	P63212 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3PVU_1 Beta-adrenergic receptor kinase 1 (chains A)
MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFS
QKLGYLLFRDFCLKHLEEAKPLVEFYEEIKKYEKLETEEERLVCSREIFDTYIMKELLAC
SHPFSKSAIEHVQGHLVKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNV
ELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER
IMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAE
IILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPE
VLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPE
LRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAA
DAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARK
KTKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSL
LTMEEIQSVEETQIKERKCLLLKIRGGKQFVLQCDSDPELVQWKKELRDAYREAQQLVQR
VPKMKNKPRAPVVELSKVPLIQRGSANGLHHHHHH

Sequence of entity 2 (B), FASTA

>3PVU_2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>3PVU_3 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains G)
HHHHHHMASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPV
PASENPFREKKFFC

Ligands and cofactors

ID	Name	Formula	Copies
QRW	3-({[4-methyl-5-(pyridin-4-yl)-4H-1,2,4-triazol-3-yl]methyl}amino)-N-[2-(triflu…	C24 H21 F3 N6 O	1

Primary citation

Molecular Mechanism of Selectivity among G Protein-Coupled Receptor Kinase 2 Inhibitors. Thal, D.M., Yeow, R.Y., Schoenau, C. et al. Mol Pharmacol (2011) 80:294-303. DOI 10.1124/mol.111.071522 · PubMed

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

3PVW 2.49 Å, Bovine GRK2 in complex with Gbetagamma subunits and a selective kinase inhibitor…
1OMW 2.5 Å, Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and…
5HE0 2.56 Å, Bovine GRK2 in complex with Gbetagamma subunits and CCG215022
3PSC 2.67 Å, Bovine GRK2 in complex with Gbetagamma subunits
5HE3 2.74 Å, Bovine GRK2 in complex with Gbetagamma subunits and CCG224411
5HE2 2.79 Å, Bovine GRK2 in complex with Gbetagamma subunits and CCG224406
8JPD 2.81 Å, Focused refinement structure of GRK2 in NTSR1-GRK2-Galpha(q) complexes
5UKM 3.03 Å, bovine GRK2 in complex with human Gbetagamma subunits and CCG258208 (14as)
2BCJ 3.06 Å, Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and…
8JPB 3.07 Å, cryo-EM structure of NTSR1-GRK2-Galpha(q) complexes 1
8JPC 3.07 Å, cryo-EM structure of NTSR1-GRK2-Galpha(q) complexes 2
3UZT 3.51 Å, Structure of the C13.18 RNA Aptamer in Complex with G Protein-Coupled Receptor Kinase 2

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