7B56

Crystal structure of CaMKII-actinin complex bound to AMPPNP

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCvkvlagqe..........YAAK

Chain	Residue	Details
B	LEU19-LYS42

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNLLL

Chain	Residue	Details
B	VAL131-LEU143

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
B	ASP135

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
B	LEU19
B	LYS42

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455

Chain	Residue	Details
B	TYR13

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11275

Chain	Residue	Details
B	SER257

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:28130356

Chain	Residue	Details
B	THR286

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