4FGB

Crystal structure of human calcium/calmodulin-dependent protein kinase I apo form

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

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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

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site_id	SWS_FT_FI2
Number of Residues	9
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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