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6TLR

HUMAN CK2 KINASE ALPHA SUBUNIT IN COMPLEX WITH THE ATP-COMPETITIVE INHIBITOR 4,7-DIBROMOBENZOTRIAZOLE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005956cellular_componentprotein kinase CK2 complex
A0006302biological_processdouble-strand break repair
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0006974biological_processDNA damage response
A0007165biological_processsignal transduction
A0008284biological_processpositive regulation of cell population proliferation
A0016055biological_processWnt signaling pathway
A0016301molecular_functionkinase activity
A0016605cellular_componentPML body
A0017148biological_processnegative regulation of translation
A0018105biological_processpeptidyl-serine phosphorylation
A0018107biological_processpeptidyl-threonine phosphorylation
A0030177biological_processpositive regulation of Wnt signaling pathway
A0030307biological_processpositive regulation of cell growth
A0031519cellular_componentPcG protein complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0042802molecular_functionidentical protein binding
A0043154biological_processnegative regulation of cysteine-type endopeptidase activity involved in apoptotic process
A0045732biological_processpositive regulation of protein catabolic process
A0048511biological_processrhythmic process
A0050821biological_processprotein stabilization
A0051726biological_processregulation of cell cycle
A0051879molecular_functionHsp90 protein binding
A0061077biological_processchaperone-mediated protein folding
A0070822cellular_componentSin3-type complex
A0075342biological_processsymbiont-mediated disruption of host cell PML body
A0106310molecular_functionprotein serine kinase activity
A1905337biological_processpositive regulation of aggrephagy
A1905818biological_processregulation of chromosome separation
A2000042biological_processnegative regulation of double-strand break repair via homologous recombination
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue NKE A 401
ChainResidue
AVAL53
AHOH736
AHOH805
AHOH814
AHOH815
ALYS68
AILE95
AVAL116
AASN118
AMET163
AILE174
AASP175
AHOH567

site_idAC2
Number of Residues10
Detailsbinding site for residue NKE A 402
ChainResidue
AVAL116
AASN117
ATHR119
AMET163
AILE164
AASP165
AARG172
AHOH530
AHOH537
AHOH837

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 403
ChainResidue
AGLN290
AVAL293
AHOH542
AHOH688
AHOH876
AHOH913

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 404
ChainResidue
APRO159
AHIS160

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VVVK
ChainResidueDetails
ALEU45-LYS68

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
AILE152-ILE164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP156

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS68
ALEU45

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CDK1 => ECO:0000269|PubMed:7592773
ChainResidueDetails
ATHR360
ATHR344

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:7592773
ChainResidueDetails
ASER362

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:7592773, ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER370

219869

PDB entries from 2024-05-15

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