5AIK

Human DYRK1A in complex with LDN-211898

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	8
Details	BINDING SITE FOR RESIDUE AWR A 900

Chain	Residue
A	PHE170
A	VAL173
A	LYS188
A	GLU203
A	PHE238
A	GLU239
A	LEU241
A	ASP307

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AWR B 900

Chain	Residue
B	PHE170
B	VAL173
B	ALA186
B	LYS188
B	GLU203
B	PHE238
B	GLU239
B	LEU241
B	SER242
B	LEU294
B	ASP307
B	GLY166

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AWR C 900

Chain	Residue
C	LYS167
C	PHE170
C	VAL173
C	ALA186
C	LYS188
C	PHE238
C	GLU239
C	LEU241
C	ASP307

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AWR D 900

Chain	Residue
D	ILE165
D	PHE170
D	VAL173
D	ALA186
D	LYS188
D	GLU203
D	PHE238
D	GLU239
D	LEU241
D	SER242
D	LEU294
D	ASP307

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 1483

Chain	Residue
B	GLY168
B	SER169
C	TYR145
C	LYS193

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 1484

Chain	Residue
B	LYS193
B	LYS194
C	SER310

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 1483

Chain	Residue
B	TYR145
B	LYS193
C	GLY168
C	SER169

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 1483

Chain	Residue
A	GLY168
A	SER169
D	TYR145
D	LYS193

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 D 1482

Chain	Residue
A	SER310
D	LYS193
D	LYS194

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 D 1483

Chain	Residue
A	TYR145
D	GLY168
D	SER169

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 1484

Chain	Residue
A	LYS264
A	ARG300
A	SER301

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 1485

Chain	Residue
B	LYS264
B	ARG300
B	SER301

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 C 1484

Chain	Residue
C	LYS264
C	ARG300
C	SER301

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 D 1484

Chain	Residue
D	LYS264
D	ARG300
D	SER301

---

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	34
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

---