3A61

Crystal structure of unphosphorylated p70S6K1 (Form II)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE STU A 400

Chain	Residue
A	LEU97
A	ASP236
A	ALA121
A	GLU173
A	TYR174
A	LEU175
A	GLU179
A	GLU222
A	ASN223
A	THR235

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGYGKVFqVrkvtgantgki.......FAMK

Chain	Residue	Details
A	LEU97-LYS123

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

Chain	Residue	Details
A	ILE214-LEU226

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP218

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

Chain	Residue	Details
A	LYS123
A	LEU97

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:19864428, ECO:0000269|PubMed:9445476

Chain	Residue	Details
A	THR252

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:19085255

Chain	Residue	Details
A	SER394

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