6KHF

Crystal structure of CLK3 in complex with CX-4945

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001669	cellular_component	acrosomal vesicle
A	0003723	molecular_function	RNA binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0006468	biological_process	protein phosphorylation
A	0016020	cellular_component	membrane
A	0016607	cellular_component	nuclear speck
A	0031410	cellular_component	cytoplasmic vesicle
A	0042802	molecular_function	identical protein binding
A	0043484	biological_process	regulation of RNA splicing
A	0045111	cellular_component	intermediate filament cytoskeleton
A	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue 3NG A 1000

Chain	Residue
A	LEU162
A	LEU290
A	ASP320
A	GLY163
A	GLU164
A	PHE167
A	ALA184
A	LYS186
A	PHE236
A	LEU238
A	LEU239

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTFGKVVeCldhargksq.........VALK

Chain	Residue	Details
A	LEU162-LYS186

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

Chain	Residue	Details
A	LEU279-PHE291

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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	ASP283

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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	LEU162
A	LYS186

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	TYR7

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER9

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER49
A	SER51

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER67

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER76
A	SER78

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER135

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