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6HMC

STRUCTURE OF PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA'; CSNK2A2 gene product) IN COMPLEX WITH THE INDENOINDOLE-TYPE INHIBITOR THN27

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000785cellular_componentchromatin
A0001669cellular_componentacrosomal vesicle
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005956cellular_componentprotein kinase CK2 complex
A0006302biological_processdouble-strand break repair
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007049biological_processcell cycle
A0007283biological_processspermatogenesis
A0016055biological_processWnt signaling pathway
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0018105biological_processpeptidyl-serine phosphorylation
A0021987biological_processcerebral cortex development
A0031519cellular_componentPcG protein complex
A0051726biological_processregulation of cell cycle
A0097421biological_processliver regeneration
A0106310molecular_functionprotein serine kinase activity
A1901524biological_processregulation of mitophagy
A1903955biological_processpositive regulation of protein targeting to mitochondrion
A1905818biological_processregulation of chromosome separation
A2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue EDO A 401
ChainResidue
AHIS184
AHOH502

site_idAC2
Number of Residues4
Detailsbinding site for residue EDO A 402
ChainResidue
AASP131
AHIS292
AVAL294
AHOH851

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 403
ChainResidue
AASP300
AHIS322
AHOH642
AHOH682
ALYS45
APRO296
AGLU297

site_idAC4
Number of Residues3
Detailsbinding site for residue EDO A 404
ChainResidue
AGLU188
AASN190
AGLN208

site_idAC5
Number of Residues8
Detailsbinding site for residue EDO A 405
ChainResidue
ALEU42
APHE55
AGLU318
AGLU321
AHIS322
AHOH511
AHOH527
AHOH547

site_idAC6
Number of Residues9
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU64
AARG65
AASP206
AASP265
AHOH506
AHOH532
AHOH536
AHOH650
AHOH919

site_idAC7
Number of Residues9
Detailsbinding site for residue EDO A 407
ChainResidue
ATYR13
AVAL16
AVAL106
AHOH728
AHOH744
AHOH764
AHOH770
AHOH779
AHOH896

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO A 408
ChainResidue
AARG22
AGLN237

site_idAC9
Number of Residues17
Detailsbinding site for residue FXB A 409
ChainResidue
ALEU46
AVAL54
AVAL67
ALYS69
AILE96
APHE114
AGLU115
AILE117
AMET164
AILE175
AASP176
AHOH514
AHOH531
AHOH657
AHOH722
AHOH819
AHOH932

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnner..........VVVK
ChainResidueDetails
ALEU46-LYS69

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
AILE153-ILE165

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
AASP157

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU46
ALYS69

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR13

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER18

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER21
ASER288

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS97

218853

PDB entries from 2024-04-24

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