6TW2

Re-refined crystal structure of di-phosphorylated human CLK1 in complex with a novel substituted indole inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue V25 E 2301

Chain	Residue
E	LEU167
E	GLU292
E	ASN293
E	LEU295
E	VAL324
E	GLY168
E	GLU169
E	VAL175
E	ALA189
E	LYS191
E	PHE241
E	GLU242
E	LEU244

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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. LGEGAFGKVVeCidhkaggrh.........VAVK

Chain	Residue	Details
E	LEU167-LYS191

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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
E	LEU284-PHE296

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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
E	ASP288

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
E	LEU167
E	LYS191

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