8R3X

Crystal structure of aPKC Iota kinase domain with LLGL2 peptide

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	0004697	molecular_function	diacylglycerol-dependent serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004697	molecular_function	diacylglycerol-dependent serine/threonine 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	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGSYAKVLlVrlkktdriyamk......VVKK

Chain	Residue	Details
A	ILE260-LYS287

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

Chain	Residue	Details
A	ILE374-LEU386

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12725730

Chain	Residue	Details
C	SER653
D	SER653

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE260
A	LYS283
B	ILE260
B	LYS283

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277, ECO:0000269|PubMed:11891849

Chain	Residue	Details
A	TYR265
B	TYR265

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277

Chain	Residue	Details
A	TYR280
A	TYR334
B	TYR280
B	TYR334

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:16125198

Chain	Residue	Details
A	TPO412
B	TPO412

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16125198, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	TPO564
B	TPO564

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
A	ASP378	proton shuttle (general acid/base)
A	LYS380	electrostatic stabiliser
A	ASN383	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
B	ASP378	proton shuttle (general acid/base)
B	LYS380	electrostatic stabiliser
B	ASN383	electrostatic stabiliser

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