6UWY

DYRK1A bound to a harmine derivative

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	11
Details	binding site for residue QKG A 501

Chain	Residue
A	ILE165
A	LEU294
A	ASP307
A	PHE170
A	ALA186
A	LYS188
A	PHE238
A	GLU239
A	MET240
A	LEU241
A	ASN244

---

site_id	AC2
Number of Residues	2
Details	binding site for residue PG4 A 502

Chain	Residue
A	TYR319
A	PTR321

---

site_id	AC3
Number of Residues	4
Details	binding site for residue PG4 A 503

Chain	Residue
A	GLY419
A	LYS422
B	ARG458
B	TYR472

---

site_id	AC4
Number of Residues	2
Details	binding site for residue PG4 A 504

Chain	Residue
A	GLN201
C	GLN201

---

site_id	AC5
Number of Residues	12
Details	binding site for residue QKG B 501

Chain	Residue
B	ILE165
B	PHE170
B	LYS188
B	PHE238
B	GLU239
B	MET240
B	LEU241
B	SER242
B	ASN244
B	LEU294
B	ASP307
D	GLN182

---

site_id	AC6
Number of Residues	4
Details	binding site for residue PG4 B 502

Chain	Residue
B	ASP162
B	LYS175
B	TRP184
B	MET240

---

site_id	AC7
Number of Residues	1
Details	binding site for residue PG4 B 503

Chain	Residue
B	PHE196

---

site_id	AC8
Number of Residues	3
Details	binding site for residue PG4 B 504

Chain	Residue
A	ARG458
A	GLN475
B	LYS422

---

site_id	AC9
Number of Residues	10
Details	binding site for residue QKG C 501

Chain	Residue
C	ILE165
C	PHE170
C	ALA186
C	LYS188
C	PHE238
C	GLU239
C	LEU241
C	ASN244
C	LEU294
C	ASP307

---

site_id	AD1
Number of Residues	3
Details	binding site for residue PG4 C 502

Chain	Residue
C	ASP162
C	LYS175
C	TRP184

---

site_id	AD2
Number of Residues	2
Details	binding site for residue PG4 C 503

Chain	Residue
C	TYR319
C	PTR321

---

site_id	AD3
Number of Residues	10
Details	binding site for residue QKG D 501

Chain	Residue
D	PHE170
D	ALA186
D	LYS188
D	PHE238
D	GLU239
D	LEU241
D	ASN244
D	GLU291
D	LEU294
D	ASP307

---

site_id	AD4
Number of Residues	3
Details	binding site for residue PG4 D 502

Chain	Residue
D	ASP162
D	LYS175
D	TRP184

---

site_id	AD5
Number of Residues	3
Details	binding site for residue PG4 D 503

Chain	Residue
D	PHE196
D	TYR319
D	PTR321

---

site_id	AD6
Number of Residues	5
Details	binding site for residue PG4 D 504

Chain	Residue
B	GLN201
B	HIS227
B	LEU234
D	GLN201
D	HIS227

---

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	136
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	48
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---