1YM7: G Protein-Coupled Receptor Kinase 2

G Protein-Coupled Receptor Kinase 2 (GRK2). Determined by X-ray diffraction at 4.5 Å resolution. Released 5 Jul 2005.

Method: X-ray diffraction
Resolution: 4.5 Å
Organism: Bos taurus
Chains: 4
Atoms: 19,846
Mol. weight: 319 kDa
Released: 5 Jul 2005

Explore 1YM7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YM7 contains 130 α-helices and 86 β-strands across 4 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: 33 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	34-36	3
α-helix	37-39	3
α-helix	40-49	10
α-helix	55-60	6
α-helix	62-74	13
α-helix	79-93	15
α-helix	98-108	11
α-helix	109-114	6
α-helix	115-118	4
α-helix	126-136	11
α-helix	147-156	10
α-helix	157-161	5
α-helix	162-166	5
α-helix	169-182	14
α-helix	188-190	3
β-strand	191-196	6	1
β-strand	205-210	6	1
β-strand	216-223	8	1
α-helix	224-229	6
α-helix	233-246	14
β-strand	254	1	2
β-strand	257-263	7	1
β-strand	266-272	7	1
β-strand	278	1	2
α-helix	279-286	8
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	359-362	4
α-helix	371-386	16
α-helix	400-408	9
α-helix	419-428	10
α-helix	444-449	6
α-helix	451-453	3
α-helix	458-462	5
α-helix	467-468	2
α-helix	503-505	3
β-strand	511-512	2	1
α-helix	514-524	11
α-helix	526-538	13
α-helix	542-545	4
β-strand	561	1	4
β-strand	564-569	6	4
β-strand	575-584	10	4
β-strand	587-591	5	4
β-strand	599-600	2	4
β-strand	608-612	5	4
β-strand	619-623	5	4
β-strand	629-633	5	4
α-helix	637-654	18

Chain B: 32 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	34-36	3
α-helix	37-39	3
α-helix	40-49	10
α-helix	55-60	6
α-helix	62-74	13
α-helix	79-93	15
α-helix	98-108	11
α-helix	109-114	6
α-helix	115-118	4
α-helix	126-136	11
α-helix	147-156	10
α-helix	157-161	5
α-helix	162-166	5
α-helix	169-182	14
α-helix	188-190	3
β-strand	191-199	9	5
β-strand	204-210	7	5
β-strand	216-223	8	5
α-helix	224-230	7
α-helix	233-246	14
β-strand	254	1	6
β-strand	257-263	7	5
β-strand	266-272	7	5
β-strand	278	1	6
α-helix	279-286	8
α-helix	291-310	20
β-strand	313-314	2	7
α-helix	320-322	3
β-strand	323-325	3	6
β-strand	331-333	3	6
β-strand	340-341	2	7
α-helix	359-362	4
α-helix	371-386	16
α-helix	400-408	9
α-helix	419-428	10
α-helix	444-449	6
α-helix	451-453	3
α-helix	458-462	5
α-helix	467-468	2
α-helix	500-503	4
β-strand	511-512	2	5
α-helix	514-524	11
α-helix	526-542	17
β-strand	561-569	9	8
β-strand	575-584	10	8
β-strand	587-591	5	8
β-strand	593	1	9
β-strand	595	1	9
β-strand	599-600	2	8
β-strand	606-612	7	10
β-strand	619-624	6	10
β-strand	629-632	4	10
β-strand	633	1	8
α-helix	637-654	18

Chain C: 33 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	34-36	3
α-helix	37-39	3
α-helix	40-49	10
α-helix	55-60	6
α-helix	62-74	13
α-helix	79-93	15
α-helix	98-108	11
α-helix	109-114	6
α-helix	115-118	4
α-helix	126-136	11
α-helix	147-156	10
α-helix	157-161	5
α-helix	162-166	5
α-helix	169-182	14
α-helix	188-190	3
β-strand	191-199	9	11
β-strand	204-210	7	11
β-strand	216-223	8	11
α-helix	224-230	7
α-helix	233-246	14
β-strand	254	1	12
β-strand	257-263	7	11
β-strand	266-272	7	11
β-strand	278	1	12
α-helix	279-286	8
α-helix	289-290	2
α-helix	291-310	20
β-strand	313-314	2	13
α-helix	320-322	3
β-strand	323-325	3	12
β-strand	331-333	3	12
β-strand	340-341	2	13
α-helix	359-362	4
α-helix	371-386	16
α-helix	400-408	9
α-helix	419-428	10
α-helix	444-449	6
α-helix	451-453	3
α-helix	458-462	5
α-helix	467-468	2
α-helix	500-503	4
β-strand	511-512	2	11
α-helix	514-524	11
α-helix	526-540	15
β-strand	561-569	9	14
β-strand	575-584	10	14
β-strand	587-591	5	14
β-strand	593	1	15
β-strand	595	1	15
β-strand	599-600	2	14
β-strand	606-612	7	16
β-strand	619-624	6	16
β-strand	629-632	4	16
β-strand	633	1	14
α-helix	637-654	18

Chain D: 32 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	34-36	3
α-helix	37-39	3
α-helix	40-49	10
α-helix	55-60	6
α-helix	62-74	13
α-helix	79-93	15
α-helix	98-108	11
α-helix	109-114	6
α-helix	115-118	4
α-helix	126-136	11
α-helix	147-156	10
α-helix	157-161	5
α-helix	162-166	5
α-helix	169-182	14
α-helix	188-190	3
β-strand	191-199	9	17
β-strand	204-210	7	17
β-strand	216-223	8	17
α-helix	224-230	7
α-helix	233-246	14
β-strand	254	1	18
β-strand	257-263	7	17
β-strand	266-272	7	17
β-strand	278	1	18
α-helix	279-286	8
α-helix	291-310	20
β-strand	313-314	2	19
α-helix	320-322	3
β-strand	323-325	3	18
β-strand	331-333	3	18
β-strand	340-341	2	19
α-helix	359-362	4
α-helix	371-386	16
α-helix	400-408	9
α-helix	419-428	10
α-helix	444-449	6
α-helix	451-453	3
α-helix	458-462	5
α-helix	467-468	2
α-helix	503-505	3
β-strand	511-512	2	17
α-helix	514-524	11
α-helix	526-538	13
β-strand	561-569	9	20
β-strand	575-584	10	20
β-strand	587-591	5	20
β-strand	593	1	21
β-strand	595	1	21
β-strand	599-600	2	20
β-strand	608-612	5	22
β-strand	619-623	5	22
β-strand	629-632	4	22
β-strand	633	1	20
α-helix	637-654	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-adrenergic receptor kinase 1	A, B, C, D	protein	689	Bos taurus	P21146 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1YM7_1 Beta-adrenergic receptor kinase 1 (chains A, B, C, D)
MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFS
QKLGYLLFRDFCLKHLEEAKPLVEFYEEIKKYEKLETEEERLVCSREIFDTYIMKELLAC
SHPFSKSAIEHVQGHLVKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNV
ELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER
IMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAE
IILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPE
VLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPE
LRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAA
DAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARK
KTKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSL
LTMEEIQSVEETQIKERKCLLLKIRGGKQFVLQCDSDPELVQWKKELRDAYREAQQLVQR
VPKMKNKPRAPVVELSKVPLIQRGSANGL

Primary citation

The role of Gbetagamma and domain interfaces in the activation of G protein-coupled receptor kinase 2. Lodowski, D.T., Barnhill, J.F., Pyskadlo, R.M. et al. Biochemistry (2005) 44:6958-6970. DOI 10.1021/bi050119q · PubMed

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

3PVU 2.48 Å, Bovine GRK2 in complex with Gbetagamma subunits and a selective kinase inhibitor (CMPD101)
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

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