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2UX0

Structure of the oligomerisation domain of calcium-calmodulin dependent protein kinase II gamma

Functional Information from GO Data
ChainGOidnamespacecontents
A0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
A0005516molecular_functioncalmodulin binding
A0006468biological_processprotein phosphorylation
B0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
B0005516molecular_functioncalmodulin binding
B0006468biological_processprotein phosphorylation
C0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
C0005516molecular_functioncalmodulin binding
C0006468biological_processprotein phosphorylation
D0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
D0005516molecular_functioncalmodulin binding
D0006468biological_processprotein phosphorylation
E0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
E0005516molecular_functioncalmodulin binding
E0006468biological_processprotein phosphorylation
F0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
F0005516molecular_functioncalmodulin binding
F0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLY A 1521
ChainResidue
AGLU430
AHIS444

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY B 1521
ChainResidue
BGLU430

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GLY C 1521
ChainResidue
CILE410
CGLU430
CHIS444

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GLY D 1521
ChainResidue
DGLU430

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GLY E 1521
ChainResidue
EHOH2017
EGLU430
EHIS444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11730","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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