Structure of PDB 3cik Chain A

Receptor sequence
>3cikA (length=619) Species: 9606 (Homo sapiens) [Search protein sequence]
SKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEE
ARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLACSHPFSKSA
TEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWK
NVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIK
MKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGD
LHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEH
GHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLG
CMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGL
LQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGTKG
IKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKKAKNK
QLGHEEDYALGKDCIMHGYMSKMTQWQRRYFYLFPNRLEWRGEGEAPQSL
LTMEEIQSVEETQIKERKCLLLKIRGGKQFILQCDSDPELVQWKKELRDA
YREAQQLVQRVPKMKNKPR
3D structure
PDB3cik Structure of human G protein-coupled receptor kinase 2 in complex with the kinase inhibitor balanol.
ChainA
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D317 K319 N322 D335 K344 T353
Catalytic site (residue number reindexed from 1) D289 K291 N294 D307 K316 T325
Enzyme Commision number 2.7.11.15: [beta-adrenergic-receptor] kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG A H348 E360 V361 Q363 V366 Y368 H320 E332 V333 Q335 V338 Y340
Gene Ontology
Molecular Function
GO:0001664 G protein-coupled receptor binding
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004703 G protein-coupled receptor kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0031694 alpha-2A adrenergic receptor binding
GO:0031755 Edg-2 lysophosphatidic acid receptor binding
GO:0047696 beta-adrenergic receptor kinase activity
Biological Process
GO:0002026 regulation of the force of heart contraction
GO:0002029 desensitization of G protein-coupled receptor signaling pathway
GO:0003108 negative regulation of the force of heart contraction by chemical signal
GO:0006468 protein phosphorylation
GO:0007165 signal transduction
GO:0007186 G protein-coupled receptor signaling pathway
GO:0007213 G protein-coupled acetylcholine receptor signaling pathway
GO:0007217 tachykinin receptor signaling pathway
GO:0007507 heart development
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0019079 viral genome replication
GO:0031623 receptor internalization
GO:0033605 positive regulation of catecholamine secretion
GO:0045988 negative regulation of striated muscle contraction
GO:0046718 symbiont entry into host cell
GO:0060048 cardiac muscle contraction
GO:1901081 negative regulation of relaxation of smooth muscle
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005929 cilium
GO:0016020 membrane
GO:0032473 cytoplasmic side of mitochondrial outer membrane
GO:0042995 cell projection
GO:0045202 synapse
GO:0098793 presynapse
GO:0098794 postsynapse

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3cik, PDBe:3cik, PDBj:3cik
PDBsum3cik
PubMed20128603
UniProtP25098|ARBK1_HUMAN Beta-adrenergic receptor kinase 1 (Gene Name=GRK2)

[Back to BioLiP]