3KL8

CaMKIINtide Inhibitor Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004860	molecular_function	protein kinase inhibitor activity
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004860	molecular_function	protein kinase inhibitor activity
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004860	molecular_function	protein kinase inhibitor activity
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004860	molecular_function	protein kinase inhibitor activity
I	0004672	molecular_function	protein kinase activity
I	0005524	molecular_function	ATP binding
I	0006468	biological_process	protein phosphorylation
J	0004860	molecular_function	protein kinase inhibitor activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU19-LYS42

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	ACT_SITE: Proton acceptor => ECO:0000305

Chain	Residue	Details
A	ASN135
C	ASN135
E	ASN135
G	ASN135
I	ASN135

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P28523, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU19
C	LEU19
E	LEU19
G	LEU19
I	LEU19

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site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:20139983

Chain	Residue	Details
A	LYS42
C	LYS42
E	LYS42
G	LYS42
I	LYS42

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