9EOY

Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CaMKII alpha hub bound to PIPA

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
A	0005516	molecular_function	calmodulin binding
A	0006468	biological_process	protein phosphorylation
B	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
B	0005516	molecular_function	calmodulin binding
B	0006468	biological_process	protein phosphorylation
C	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
C	0005516	molecular_function	calmodulin binding
C	0006468	biological_process	protein phosphorylation
D	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
D	0005516	molecular_function	calmodulin binding
D	0006468	biological_process	protein phosphorylation
E	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
E	0005516	molecular_function	calmodulin binding
E	0006468	biological_process	protein phosphorylation
F	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
F	0005516	molecular_function	calmodulin binding
F	0006468	biological_process	protein phosphorylation
G	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
G	0005516	molecular_function	calmodulin binding
G	0006468	biological_process	protein phosphorylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11798","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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