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2ACX

Crystal Structure of G protein coupled receptor kinase 6 bound to AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004703molecular_functionG protein-coupled receptor kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0008277biological_processregulation of G protein-coupled receptor signaling pathway
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0016055biological_processWnt signaling pathway
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0047696molecular_functionbeta-adrenergic receptor kinase activity
B0000166molecular_functionnucleotide binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004703molecular_functionG protein-coupled receptor kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0008277biological_processregulation of G protein-coupled receptor signaling pathway
B0009966biological_processregulation of signal transduction
B0016020cellular_componentmembrane
B0016055biological_processWnt signaling pathway
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0047696molecular_functionbeta-adrenergic receptor kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 578
ChainResidue
AANP577

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 578
ChainResidue
BANP577

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 579
ChainResidue
AALA15
AARG16
ASER27
AARG187
AARG206

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 579
ChainResidue
BSER27
BARG187
BARG206
BALA15
BARG16

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ANP A 577
ChainResidue
AARG123
ALYS194
AGLY195
AGLY196
AVAL200
AALA213
ALYS215
ATHR264
AMET266
ALEU318
AASP329
AMG578

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ANP B 577
ChainResidue
BARG123
BLYS194
BGLY195
BGLY196
BVAL200
BALA213
BLYS215
BTHR264
BMET266
BASP329
BMG578

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues33
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFGEVCaCqvratgkmyackklekk.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 Residues236
DetailsDomain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues262
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP311
AGLU315

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP311
BGLU315

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP311
ALYS313

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP311
BLYS313

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR348
AASP311
ALYS313

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR348
BASP311
BLYS313

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN316
AASP311
ALYS313

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN316
BASP311
BLYS313

245011

PDB entries from 2025-11-19

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