6FYL

X-ray structure of CLK2-KD(136-496)/CX-4945 at 1.95A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein 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 3NG A 501

Chain	Residue
A	LEU169
A	LEU297
A	VAL326
A	ASP327
A	HOH611
A	HOH634
A	HOH788
A	GLY170
A	GLU171
A	PHE174
A	ALA191
A	LYS193
A	PHE243
A	GLU244
A	LEU246

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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. LGEGTFGRVVqCvdhrrggar.........VALK

Chain	Residue	Details
A	LEU169-LYS193

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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	LEU286-PHE298

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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	LEU291

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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	GLY170
A	ILE194

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	VAL143

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	HIS154

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PKB/AKT2 => ECO:0000250|UniProtKB:O35491

Chain	Residue	Details
A	ARG345

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