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5CVG

Crystal Structure of CK2alpha with a novel closed conformation of the aD loop

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ACT A 401
ChainResidue
ALYS68
AILE95
AASP175
AHOH612
AHOH628

site_idAC2
Number of Residues3
Detailsbinding site for residue ACT A 402
ChainResidue
AARG80
AARG155
AHOH693

site_idAC3
Number of Residues3
Detailsbinding site for residue ACT A 403
ChainResidue
AASP103
AARG280
AGLN36

site_idAC4
Number of Residues5
Detailsbinding site for residue ACT A 404
ChainResidue
ATHR13
AARG228
AHIS291
AHOH650
AHOH701

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
ALEU45
ALYS68

226707

PDB entries from 2024-10-30

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