7OY6

Crystal structure of human DYRK1A in complex with ARN25068

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0004672	molecular_function	protein kinase activity
C	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0046777	biological_process	protein autophosphorylation

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ILE165-LYS188

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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
C	ILE283-LEU295

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168

Chain	Residue	Details
C	ASP287

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

Chain	Residue	Details
C	LYS188
C	PHE238
C	ILE165

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site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
C	TYR159
C	TYR177
C	TYR319
C	PTR321
C	TYR449
C	TYR140

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

Chain	Residue	Details
C	TYR145

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470

Chain	Residue	Details
C	TYR219

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
C	SER310

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
C	THR402

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