1ZRZ

Crystal Structure of the Catalytic Domain of Atypical Protein Kinase C-iota

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	15
Details	BINDING SITE FOR RESIDUE BI1 A 1000

Chain	Residue
A	ILE251
A	VAL326
A	ASP330
A	ASP373
A	LEU376
A	THR386
A	ASP387
A	GLY252
A	VAL259
A	ALA272
A	LYS274
A	VAL307
A	ILE323
A	GLU324
A	TYR325

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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. IGRGSYAKVLlVrlkktdriyamk......VVKK

Chain	Residue	Details
A	ILE251-LYS278

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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	ILE365-LEU377

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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	ASP378

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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	LEU260
A	ASP283

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277, ECO:0000269|PubMed:11891849

Chain	Residue	Details
A	LYS265

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:11713277

Chain	Residue	Details
A	LEU280
A	HIS334

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:16125198

Chain	Residue	Details
A	ALA412

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:16125198, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	LYS564

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 16125198

Chain	Residue	Details
A	ASN374
A	ASP369
A	LYS371

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 756

Chain	Residue	Details
A	ASP378	proton shuttle (general acid/base)
A	GLU380	electrostatic stabiliser
A	ILE383	electrostatic stabiliser

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