4DC2

Structure of PKC in Complex with a Substrate Peptide from Par-3

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ADE A 601

Chain	Residue
A	ILE322
A	GLU323
A	VAL325
A	LEU375
A	THR385
A	PHE542

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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. IGRGSYAKVLlVrlkktdriyamr......VVKK

Chain	Residue	Details
A	ILE250-LYS277

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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	ILE364-LEU376

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:12045219, ECO:0000269|PubMed:22579248

Chain	Residue	Details
Z	SER1060

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99NH2

Chain	Residue	Details
A	ARG273
Z	LYS1067

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8TEW0

Chain	Residue	Details
A	TYR270
A	TYR324
Z	SER1070

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17242355

Chain	Residue	Details
A	THR402

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:22579248, ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	TPO554

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