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2CHL

Structure of casein kinase 1 gamma 3

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 SO4 A 1324
ChainResidue
APRO272
AILE273
AGLU274
AARG288
AHOH2253
AHOH2254

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1325
ChainResidue
AARG260
AHOH2255
AHOH2256
AARG214
AGLN250
AGLY251

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1326
ChainResidue
ALYS110
ASER135
ALEU136
AHOH2257
AHOH2258
AHOH2259

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1327
ChainResidue
AARG161
ALYS190
ALYS207
AGLU225

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1328
ChainResidue
AARG228
ALYS298
AHOH2260

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE DKI A 1323
ChainResidue
AILE49
APHE54
ALEU57
AALA70
AGLU117
ALEU118
ALEU119
AGLY120
AGLU166
AASN167
ALEU169
AILE184
AASP185
APRO331
ATHR332
APRO333
AHOH2252

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 Residues270
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
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_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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
AGLU155
AASP151

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP151
ALYS153

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR201
AASP151
ALYS153

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN156
AASP151
ALYS153

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PDB entries from 2025-12-24

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