6CZ4

Structure of the PTK6 kinase domain bound to a type II inhibitor 2-{[(3R,4S)-3-fluoro-1-{[4-(trifluoromethoxy)phenyl]acetyl}piperidin-4-yl]oxy}-5-(1-methyl-1H-imidazol-4-yl)pyridine-3-carboxamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine 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	20
Details	binding site for residue FKY A 9001

Chain	Residue
A	LEU197
A	MET267
A	ALA268
A	GLY270
A	LEU303
A	TYR308
A	HIS310
A	VAL328
A	GLY329
A	ASP330
A	PHE331
A	ALA217
A	HOH9193
A	MET239
A	LEU242
A	ILE247
A	LEU248
A	THR264
A	GLU265
A	LEU266

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGYFGEVFeGlwkdrvq...........VAIK

Chain	Residue	Details
A	LEU197-LYS219

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site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YIHrDLAARNILV

Chain	Residue	Details
A	TYR308-VAL320

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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:PRU10028

Chain	Residue	Details
A	ASP312

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU197

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:27480927, ECO:0000305|PubMed:27993680

Chain	Residue	Details
A	LYS219

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12121988

Chain	Residue	Details
A	TYR342
A	TYR351

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