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2IZU

Structure of casein kinase gamma 3 in complex with inhibitor

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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A1337
ChainResidue
AARG214
AGLN250
AGLY251
AARG260
AHOH2360
AHOH2361

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE P01 A1335
ChainResidue
AGLU117
ALEU119
AGLY120
AGLU166
ALEU169
AILE184
APRO331
ATHR332
APRO333
AHOH2124
AHOH2359
AILE49
ALEU57
AALA70

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A1336
ChainResidue
ATYR289
AASP300
ATYR303
AHOH2298

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGCGNFGELRlGknlytney..........VAIK
ChainResidueDetails
AILE49-LYS72

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDVKpeNFLI
ChainResidueDetails
ALEU158-ILE170

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
AASP162

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE49
ALYS72

218853

PDB entries from 2024-04-24

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