Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MQ1

The crystal structure of DYRK1a with a bound pyrido[2,3-d]pyrimidine 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	19
Details	BINDING SITE FOR RESIDUE 2C3 A 501

Chain	Residue
A	ILE165
A	GLU239
A	MET240
A	LEU241
A	SER242
A	ASN292
A	LEU294
A	VAL306
A	ASP307
A	SO4505
A	HOH676
A	GLY166
A	LYS167
A	GLY168
A	PHE170
A	GLY171
A	VAL173
A	LYS188
A	PHE238

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 1PE A 502

Chain	Residue
A	ASP162
A	LYS175
A	TRP184

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 1PE A 503

Chain	Residue
A	GLN201
C	GLN201
C	LEU234

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 504

Chain	Residue
A	THR466
A	ARG467
A	ILE468
A	GLN469
A	TYR472

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 505

Chain	Residue
A	GLY168
A	SER169
A	LYS289
A	GLY411
A	2C3501
A	HOH758
A	HOH782

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 2C3 B 501

Chain	Residue
B	ILE165
B	LYS167
B	GLY168
B	GLY171
B	GLN172
B	LYS188
B	PHE238
B	GLU239
B	MET240
B	LEU241
B	SER242
B	TYR243
B	ASN292
B	LEU294
B	VAL306
B	ASP307
B	1PE502
B	HOH637
B	HOH700
D	GLN182

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 1PE B 502

Chain	Residue
B	ASP162
B	LYS175
B	TRP184
B	2C3501

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE 1PE B 503

Chain	Residue
B	GLN201
B	MET229
D	GLN201

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 504

Chain	Residue
B	LYS264
B	ARG300
B	SER301

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 505

Chain	Residue
B	ARG467
B	ILE468
B	GLN469
B	TYR472

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 2C3 C 501

Chain	Residue
C	ILE165
C	LYS167
C	GLY168
C	GLY171
C	VAL173
C	LYS188
C	PHE238
C	GLU239
C	MET240
C	LEU241
C	SER242
C	TYR243
C	ASN292
C	LEU294
C	VAL306
C	ASP307
C	1PE502
C	SO4503

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1PE C 502

Chain	Residue
C	ASP162
C	LYS175
C	TRP184
C	2C3501
C	HOH615

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 503

Chain	Residue
C	GLY168
C	SER169
C	2C3501
C	HOH619

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 504

Chain	Residue
C	ASN365
C	GLU366
C	LYS393
C	PTR321

site_id	BC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 2C3 D 501

Chain	Residue
D	ILE165
D	LYS167
D	GLY168
D	PHE170
D	GLY171
D	VAL173
D	LYS188
D	PHE238
D	GLU239
D	MET240
D	LEU241
D	SER242
D	ASN292
D	LEU294
D	ASP307
D	1PE502
D	SO4503

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 1PE D 502

Chain	Residue
D	ASP162
D	LYS175
D	TRP184
D	2C3501
D	HOH650
D	HOH651

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 503

Chain	Residue
D	GLY168
D	SER169
D	LYS289
D	2C3501

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 504

Chain	Residue
D	PTR321
D	GLU366
D	LYS393

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)