7EJV

The co-crystal structure of DYRK2 with YK-2-69

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydhkvhqh..........VALK

Chain	Residue	Details
B	ILE155-LYS178
A	ILE155-LYS178

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

Chain	Residue	Details
B	ILE271-LEU283
A	ILE271-LEU283

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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
B	ASP275

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
B	ILE155
B	LYS178
B	PHE228

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by MAP3K10 => ECO:0000269|PubMed:18455992

Chain	Residue	Details
B	THR308

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:22998443

Chain	Residue	Details
B	PTR309

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by ATM => ECO:0000269|PubMed:19965871

Chain	Residue	Details
B	SER369

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by MAP3K10 => ECO:0000269|PubMed:18455992

Chain	Residue	Details
B	SER376

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