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8XY7

hPhK alpha-gamma subcomplex in active state

Functional Information from GO Data
ChainGOidnamespacecontents
A0004689molecular_functionphosphorylase kinase activity
A0005516molecular_functioncalmodulin binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005964cellular_componentphosphorylase kinase complex
A0005975biological_processcarbohydrate metabolic process
A0005977biological_processglycogen metabolic process
A0006091biological_processgeneration of precursor metabolites and energy
A0045819biological_processpositive regulation of glycogen catabolic process
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004689molecular_functionphosphorylase kinase activity
C0005516molecular_functioncalmodulin binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0005964cellular_componentphosphorylase kinase complex
C0005975biological_processcarbohydrate metabolic process
C0005977biological_processglycogen metabolic process
C0006338biological_processchromatin remodeling
C0006468biological_processprotein phosphorylation
C0016310biological_processphosphorylation
C0019899molecular_functionenzyme binding
C0044024molecular_functionhistone H2AS1 kinase activity
C0050321molecular_functiontau-protein kinase activity
C0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGVSSVVRrCihkptsqe..........YAVK
ChainResidueDetails
CLEU26-LYS49

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILL
ChainResidueDetails
CILE146-LEU158

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
CASP150
ASER1113

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CLEU26
CLYS49

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER735

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER758

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER972
ASER985

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P18688
ChainResidueDetails
ASER1007

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P18688
ChainResidueDetails
ASER1018

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18688
ChainResidueDetails
ASER1020
ASER1023

site_idSWS_FT_FI9
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000250|UniProtKB:P18688
ChainResidueDetails
ACYS1220

226707

PDB entries from 2024-10-30

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