4FG8

Crystal structure of human calcium/calmodulin-dependent protein kinase I 1-315 in complex with ATP

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	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 401

Chain	Residue
A	LEU26
A	VAL98
A	GLU102
A	GLU145
A	ASN146
A	LEU148
A	SER161
A	HOH503
A	HOH514
A	HOH546
A	GLY29
A	ALA30
A	SER32
A	VAL34
A	ALA47
A	LYS49
A	VAL79
A	GLN96

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ATP B 401

Chain	Residue
B	GLY27
B	THR28
B	GLY29
B	SER32
B	VAL34
B	ALA47
B	LYS49
B	VAL79
B	GLN96
B	VAL98
B	ASN146
B	HOH536

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVIlAedkrtqklvaik......CIAK

Chain	Residue	Details
A	LEU26-LYS53

---

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

Chain	Residue	Details
A	ILE137-TYR149

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CaMKK1 and CaMKK2","evidences":[{"source":"PubMed","id":"7641687","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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