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5M4U

ORTHORHOMBIC COMPLEX STRUCTURE OF HUMAN PROTEIN KINASE CK2 CATALYTIC SUBUNIT (ISOFORM CK2ALPHA') WITH THE INHIBITOR 4'-CARBOXY-6,8-CHLORO- FLAVONOL (FLC21)

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0007283biological_processspermatogenesis
A0016055biological_processWnt signaling pathway
A0021987biological_processcerebral cortex development
A0031519cellular_componentPcG protein complex
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
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
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 7FC A 401
ChainResidue
AARG48
AILE175
AASP176
AHOH542
AHOH646
AVAL67
ALYS69
AILE96
APHE114
AGLU115
ATYR116
AILE117
AMET164

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 402
ChainResidue
ATRP34
ALYS80
ALYS103
AHOH717

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
AARG9
AALA10
AALA14
AHOH501

site_idAC4
Number of Residues5
Detailsbinding site for residue GOL A 404
ChainResidue
ATRP25
AHIS184
AGLN187
AACT408
AHOH527

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 405
ChainResidue
AHIS277
ASER278
ALYS280
AHOH505
AHOH536
AHOH553

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL A 406
ChainResidue
APHE122
ALYS123
AHIS161
AGLU231
AHOH651
AHOH672
AHOH682

site_idAC7
Number of Residues4
Detailsbinding site for residue ACT A 407
ChainResidue
AGLU15
ASER18
ALEU19
AASN284

site_idAC8
Number of Residues4
Detailsbinding site for residue ACT A 408
ChainResidue
AASP26
ATYR27
AGLU28
AGOL404

site_idAC9
Number of Residues2
Detailsbinding site for residue ACT A 409
ChainResidue
AARG192
ALYS199

site_idAD1
Number of Residues2
Detailsbinding site for residue CL A 410
ChainResidue
AGLU87
AARG90

site_idAD2
Number of Residues6
Detailsbinding site for residue SO4 A 411
ChainResidue
AARG81
AARG156
AASN190
AHOH552
AHOH628
AHOH657

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

223532

PDB entries from 2024-08-07

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