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4WNK

Crystal Structure of Bovine G Protein Coupled-Receptor Kinase 5 in Complex with CCG215022

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004703molecular_functionG protein-coupled receptor kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0008289molecular_functionlipid binding
A0009966biological_processregulation of signal transduction
A0016055biological_processWnt signaling pathway
A0043066biological_processnegative regulation of apoptotic process
A0046777biological_processprotein autophosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 453 A 701
ChainResidue
ALEU192
ALYS215
ALEU217
AMET230
AGLU234
ATHR264
AILE265
AMET266
AGLU315
AASN316
ALEU318
AGLY193
ASER328
AASP329
AHOH804
AHOH817
ALYS194
AGLY195
AGLY196
APHE197
AGLY198
AVAL200
AALA213

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 702
ChainResidue
ALYS183
ATHR255
ALYS256
AHOH837

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues33
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFGEVCaCqvratgkmyackrlekk.RIKK
ChainResidueDetails
ALEU192-LYS224

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL
ChainResidueDetails
AILE307-LEU319

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP311

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:8120045
ChainResidueDetails
ASER484

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8120045
ChainResidueDetails
ATHR485

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8VEB1
ChainResidueDetails
ASER613

222415

PDB entries from 2024-07-10

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