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2IZR

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 MG A1336
ChainResidue
AHOH2062
AHOH2063
AHOH2119
AHOH2138
AHOH2139
AHOH2165

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A1337
ChainResidue
AHOH2274
AHOH2286
AHOH2287
AASP185
AHOH2263
AHOH2269

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A1338
ChainResidue
ALYS137
ATYR317
AMET318
AHOH2110

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A1339
ChainResidue
ALYS61
AARG149
AHOH2123

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A1340
ChainResidue
AARG214
AGLN250
AARG260
AHOH2352

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A1341
ChainResidue
AGLU67
ATYR68
AARG172

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BRK A1335
ChainResidue
AASN53
ALEU57
ALEU116
AGLU117
ALEU118
ALEU119
AGLY120
AILE184
AHOH2060

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO A1342
ChainResidue
AGLY50
AASN53
AASP125
AHOH2174
AHOH2181

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLU166
AASP162

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS164
AASP162

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR212
ALYS164
AASP162

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS164
AASN167
AASP162

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PDB entries from 2025-10-22

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