6T6A

Crystal structure of DYRK1A complexed with KuFal319 (compound 11)

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 PG4 A 501

Chain	Residue
A	GLN201
A	HIS227
A	HOH660
C	GLN201
C	MET229

---

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

Chain	Residue
A	SER324
A	PHE196
A	TYR319
A	PTR321
A	GLN323

---

site_id	AC3
Number of Residues	2
Details	binding site for residue PG4 A 503

Chain	Residue
A	LYS175
A	TRP184

---

site_id	AC4
Number of Residues	6
Details	binding site for residue SO4 A 504

Chain	Residue
A	ARG255
A	GLY256
A	SER258
A	ARG438
A	HOH633
A	HOH636

---

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 505

Chain	Residue
A	ARG467
A	ILE468
A	GLN469
A	TYR472

---

site_id	AC6
Number of Residues	3
Details	binding site for residue SO4 A 506

Chain	Residue
A	GLU181
A	LYS225
A	ARG226

---

site_id	AC7
Number of Residues	6
Details	binding site for residue MLW A 507

Chain	Residue
A	PHE170
A	ALA186
A	GLU239
A	ASP307
A	HOH622
A	HOH626

---

site_id	AC8
Number of Residues	4
Details	binding site for residue PG4 B 501

Chain	Residue
B	GLN201
B	HIS227
D	GLN201
D	HIS227

---

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 B 502

Chain	Residue
B	ARG458
B	ARG467
B	ILE468
B	GLN469
B	TYR472

---

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 B 503

Chain	Residue
B	LYS264
B	ARG300
B	SER301

---

site_id	AD2
Number of Residues	2
Details	binding site for residue SO4 B 504

Chain	Residue
B	SER258
B	ASN260

---

site_id	AD3
Number of Residues	2
Details	binding site for residue SO4 B 505

Chain	Residue
B	GLU181
B	ARG226

---

site_id	AD4
Number of Residues	5
Details	binding site for residue MLW B 506

Chain	Residue
B	PHE170
B	ALA186
B	GLU239
B	LEU241
B	LEU294

---

site_id	AD5
Number of Residues	4
Details	binding site for residue PG4 C 501

Chain	Residue
C	ASP162
C	LYS175
C	TRP184
C	MET240

---

site_id	AD6
Number of Residues	3
Details	binding site for residue SO4 C 502

Chain	Residue
C	LYS264
C	ARG300
C	SER301

---

site_id	AD7
Number of Residues	2
Details	binding site for residue SO4 C 503

Chain	Residue
C	SER258
C	ASN260

---

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 C 504

Chain	Residue
C	ARG255
C	GLY256
C	SER258
C	ARG438

---

site_id	AD9
Number of Residues	3
Details	binding site for residue SO4 C 505

Chain	Residue
C	LYS225
C	ARG226
C	HOH641

---

site_id	AE1
Number of Residues	7
Details	binding site for residue MLW C 506

Chain	Residue
C	PHE170
C	VAL173
C	ALA186
C	LYS188
C	PHE238
C	GLU239
C	ASP307

---

site_id	AE2
Number of Residues	3
Details	binding site for residue SO4 D 501

Chain	Residue
D	LYS264
D	ARG300
D	SER301

---

site_id	AE3
Number of Residues	3
Details	binding site for residue SO4 D 502

Chain	Residue
D	ARG158
D	GLU181
D	ARG226

---

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

---