6S1I

Crystal Structure of DYRK1A with small molecule inhibitor

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	5
Details	binding site for residue SO4 A 501

Chain	Residue
A	ASN365
A	GLU366
A	VAL367
A	LYS393
A	HOH695

---

site_id	AC2
Number of Residues	5
Details	binding site for residue PG4 A 502

Chain	Residue
A	HOH703
A	ASP162
A	LYS175
A	TRP184
A	MET240

---

site_id	AC3
Number of Residues	11
Details	binding site for residue KR8 A 503

Chain	Residue
A	ILE165
A	PHE170
A	LYS188
A	PHE238
A	GLU239
A	MET240
A	LEU241
A	SER242
A	LEU294
A	ASP307
A	HOH625

---

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 B 501

Chain	Residue
B	LYS264
B	ARG300
B	SER301
B	HOH663

---

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 B 502

Chain	Residue
B	PTR321
B	ARG325
B	ARG328
B	HOH638

---

site_id	AC6
Number of Residues	4
Details	binding site for residue PG4 B 503

Chain	Residue
A	GLN201
A	LEU234
B	GLN201
B	HIS227

---

site_id	AC7
Number of Residues	5
Details	binding site for residue PG4 B 504

Chain	Residue
B	ASP162
B	ILE165
B	LYS175
B	TRP184
B	HOH605

---

site_id	AC8
Number of Residues	11
Details	binding site for residue KR8 B 505

Chain	Residue
B	GLY166
B	PHE170
B	LYS188
B	PHE238
B	GLU239
B	LEU241
B	SER242
B	LEU294
B	VAL306
B	ASP307
B	HOH618

---

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 C 501

Chain	Residue
C	LYS264
C	ARG300
C	SER301
D	LYS407

---

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 C 502

Chain	Residue
C	ARG325
C	ARG328
C	HOH607

---

site_id	AD2
Number of Residues	4
Details	binding site for residue PG4 C 503

Chain	Residue
C	GLN201
C	HOH604
D	GLN201
D	VAL204

---

site_id	AD3
Number of Residues	3
Details	binding site for residue PG4 C 504

Chain	Residue
C	ASP162
C	LYS175
C	TRP184

---

site_id	AD4
Number of Residues	10
Details	binding site for residue KR8 C 505

Chain	Residue
C	PHE170
C	ALA186
C	LYS188
C	PHE238
C	GLU239
C	LEU241
C	SER242
C	LEU294
C	ASP307
C	HOH609

---

site_id	AD5
Number of Residues	4
Details	binding site for residue SO4 D 501

Chain	Residue
D	LYS264
D	ARG300
D	SER301
D	HOH662

---

site_id	AD6
Number of Residues	1
Details	binding site for residue SO4 D 502

Chain	Residue
D	ARG226

---

site_id	AD7
Number of Residues	11
Details	binding site for residue KR8 D 503

Chain	Residue
D	PHE170
D	VAL173
D	ALA186
D	LYS188
D	PHE238
D	GLU239
D	MET240
D	LEU241
D	LEU294
D	ASP307
D	HOH610

---

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

---

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

---