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8UAQ

Crystal Structure of Human G Protein-Coupled Receptor Kinase 5 in Complex with GRL018-21

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004703molecular_functionG protein-coupled receptor kinase activity
A0005080molecular_functionprotein kinase C binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005543molecular_functionphospholipid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007217biological_processtachykinin receptor signaling pathway
A0008277biological_processregulation of G protein-coupled receptor signaling pathway
A0008284biological_processpositive regulation of cell population proliferation
A0008289molecular_functionlipid binding
A0009966biological_processregulation of signal transduction
A0016055biological_processWnt signaling pathway
A0016607cellular_componentnuclear speck
A0031965cellular_componentnuclear membrane
A0043066biological_processnegative regulation of apoptotic process
A0045444biological_processfat cell differentiation
A0046777biological_processprotein autophosphorylation
A0047696molecular_functionbeta-adrenergic receptor kinase activity
A0051726biological_processregulation of cell cycle
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues33
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFGEVCaCqvratgkmyackrlekk.RIKK
ChainResidueDetails
ALEU192-LYS224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASN311

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU192
ALYS215

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:8144599, ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER484

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8144599, ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR485

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8VEB1
ChainResidueDetails
ASER579

222415

PDB entries from 2024-07-10

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