Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5YF9

Crystal structure of CK2a2 form-2

Functional Information from GO Data
ChainGOidnamespacecontents
B0000785cellular_componentchromatin
B0001669cellular_componentacrosomal vesicle
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005956cellular_componentprotein kinase CK2 complex
B0006302biological_processdouble-strand break repair
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0007283biological_processspermatogenesis
B0016055biological_processWnt signaling pathway
B0021987biological_processcerebral cortex development
B0031519cellular_componentPcG protein complex
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0051726biological_processregulation of cell cycle
B0097421biological_processliver regeneration
B0106310molecular_functionprotein serine kinase activity
B1901524biological_processregulation of mitophagy
B1903955biological_processpositive regulation of protein targeting to mitochondrion
B1905818biological_processregulation of chromosome separation
B2001234biological_processnegative regulation of apoptotic signaling pathway
X0000785cellular_componentchromatin
X0001669cellular_componentacrosomal vesicle
X0004672molecular_functionprotein kinase activity
X0004674molecular_functionprotein serine/threonine kinase activity
X0005515molecular_functionprotein binding
X0005524molecular_functionATP binding
X0005634cellular_componentnucleus
X0005654cellular_componentnucleoplasm
X0005737cellular_componentcytoplasm
X0005829cellular_componentcytosol
X0005956cellular_componentprotein kinase CK2 complex
X0006302biological_processdouble-strand break repair
X0006468biological_processprotein phosphorylation
X0006915biological_processapoptotic process
X0007283biological_processspermatogenesis
X0016055biological_processWnt signaling pathway
X0021987biological_processcerebral cortex development
X0031519cellular_componentPcG protein complex
X0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
X0051726biological_processregulation of cell cycle
X0097421biological_processliver regeneration
X0106310molecular_functionprotein serine kinase activity
X1901524biological_processregulation of mitophagy
X1903955biological_processpositive regulation of protein targeting to mitochondrion
X1905818biological_processregulation of chromosome separation
X2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue NIO X 401
ChainResidue
XVAL67
XLYS69
XPHE114
XILE175
XASP176
XHOH585
XHOH610
XHOH621

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 X 402
ChainResidue
XARG81
XARG156
XASN190
XHOH508
XHOH561
XHOH712
XHOH737
XLYS78

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 X 403
ChainResidue
XARG307
XTYR308
XASP309
XHOH560
XHOH572
XHOH591
XHOH626
XHOH769

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 X 404
ChainResidue
XLYS171
XARG173
XHOH657

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 X 405
ChainResidue
XHIS287
XSER288
XARG291
XHOH725
XHOH763

site_idAC6
Number of Residues9
Detailsbinding site for residue SO4 X 406
ChainResidue
BARG192
BHOH721
XLYS199
XASN239
XHOH507
XHOH511
XHOH535
XHOH612
XHOH617

site_idAC7
Number of Residues5
Detailsbinding site for residue NIO B 401
ChainResidue
BLYS69
BPHE114
BILE175
BASP176
BHOH549

site_idAC8
Number of Residues8
Detailsbinding site for residue SO4 B 402
ChainResidue
BLYS78
BARG81
BARG156
BASN190
BHOH516
BHOH521
BHOH553
BHOH587

site_idAC9
Number of Residues7
Detailsbinding site for residue SO4 B 403
ChainResidue
BARG307
BASP309
BHOH531
BHOH564
BHOH664
BHOH724
BHOH744

site_idAD1
Number of Residues8
Detailsbinding site for residue SO4 B 404
ChainResidue
BARG192
BLYS199
BASN239
BHOH608
BHOH771
BHOH786
XARG192
XHOH507

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnner..........VVVK
ChainResidueDetails
XLEU46-LYS69

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVMI
ChainResidueDetails
XILE153-ILE165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
XASP157
BASP157

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
XLEU46
XLYS69
BLEU46
BLYS69

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
XTYR13
BTYR13

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
XSER18
BSER18

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
XSER21
XSER288
BSER21
BSER288

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
XLYS97
BLYS97

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon