3ANQ

human DYRK1A/inhibitor complex

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
A	0046777	biological_process	protein autophosphorylation
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
B	0046777	biological_process	protein autophosphorylation
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
D	0004672	molecular_function	protein kinase activity
D	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0046777	biological_process	protein autophosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EHB A 1

Chain	Residue
A	PHE170
A	ALA186
A	LYS188
A	GLU239
A	LEU241
A	LEU294
A	ASP307

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EHB B 1

Chain	Residue
B	PHE238
B	GLU239
B	LEU241
B	LEU294
B	ASP307
B	ALA186
B	LYS188

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EHB C 1

Chain	Residue
C	PHE170
C	ALA186
C	LYS188
C	GLU239
C	LEU241
C	LEU294
C	ASP307

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EHB D 1

Chain	Residue
D	PHE170
D	ALA186
D	LYS188
D	GLU239
D	LEU241
D	LEU294
D	ASP307

---

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
A	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
A	ILE283-LEU295

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:23665168

Chain	Residue	Details
A	ASP287
B	ASP287
C	ASP287
D	ASP287

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ILE165
D	ILE165
D	LYS188
D	PHE238
A	LYS188
A	PHE238
B	ILE165
B	LYS188
B	PHE238
C	ILE165
C	LYS188
C	PHE238

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
A	TYR140
B	TYR319
B	PTR321
B	TYR449
C	TYR140
C	TYR159
C	TYR177
C	TYR319
C	PTR321
C	TYR449
D	TYR140
A	TYR159
D	TYR159
D	TYR177
D	TYR319
D	PTR321
D	TYR449
A	TYR177
A	TYR319
A	PTR321
A	TYR449
B	TYR140
B	TYR159
B	TYR177

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	TYR145
B	TYR145
C	TYR145
D	TYR145

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000250|UniProtKB:Q63470

Chain	Residue	Details
A	TYR219
B	TYR219
C	TYR219
D	TYR219

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
A	SER310
B	SER310
C	SER310
D	SER310

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23665168

Chain	Residue	Details
A	THR402
B	THR402
C	THR402
D	THR402

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