Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2VX3

Crystal structure of the human dual specificity tyrosine- phosphorylation-regulated kinase 1A

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	18
Details	BINDING SITE FOR RESIDUE D15 A 600

Chain	Residue
A	GLY166
A	LEU241
A	SER242
A	ASN292
A	LEU294
A	ASP307
A	CL620
A	P6G700
A	SO41483
A	HOH2035
A	LYS167
A	GLY168
A	GLY171
A	GLN172
A	VAL173
A	ALA186
A	GLU239
A	MET240

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 620

Chain	Residue
A	LYS188
A	ASP307
A	D15600

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE P6G A 700

Chain	Residue
A	ASP162
A	LYS175
A	D15600

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE P6G A 701

Chain	Residue
A	GLN201
C	GLN201

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE P6G A 702

Chain	Residue
A	TYR319

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE D15 B 600

Chain	Residue
B	ILE165
B	GLY166
B	GLY168
B	GLY171
B	GLN172
B	VAL173
B	ALA186
B	LYS188
B	GLU239
B	LEU241
B	SER242
B	ASN292
B	LEU294
B	ASP307
B	CL620
B	P6G700
B	SO41482
D	ARG179

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 620

Chain	Residue
B	LYS188
B	ASP307
B	D15600

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE P6G B 700

Chain	Residue
B	ASP162
B	LYS175
B	MET240
B	D15600

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE P6G B 701

Chain	Residue
B	GLN201
B	HIS227
D	GLN201
D	LEU234

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE P6G B 702

Chain	Residue
B	ASP247
B	ASN251
D	GLU160

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE D15 C 600

Chain	Residue
C	ILE165
C	GLY166
C	LYS167
C	GLY168
C	GLY171
C	VAL173
C	ALA186
C	LYS188
C	GLU239
C	MET240
C	LEU241
C	SER242
C	ASN292
C	LEU294
C	ASP307
C	CL620
C	SO41482

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 620

Chain	Residue
C	LYS188
C	ASP307
C	D15600

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE P6G C 700

Chain	Residue
C	ASP162
C	LYS175
C	TRP184

site_id	BC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE D15 D 600

Chain	Residue
D	SO41482
D	ILE165
D	GLY166
D	LYS167
D	GLY168
D	GLY171
D	GLN172
D	VAL173
D	ALA186
D	GLU239
D	MET240
D	LEU241
D	SER242
D	TYR243
D	ASN292
D	LEU294
D	ASP307
D	CL620

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 620

Chain	Residue
D	LYS188
D	ASP307
D	D15600

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE P6G D 700

Chain	Residue
D	ASP162
D	LYS175
D	TRP184

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 1482

Chain	Residue
C	GLY168
C	SER169
C	LYS289
C	D15600
C	HOH2026

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 1483

Chain	Residue
A	GLY168
A	SER169
A	LYS289
A	ASP307
A	ASP410
A	D15600

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 1482

Chain	Residue
C	ASP410
D	GLY168
D	SER169
D	LYS289
D	D15600

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1482

Chain	Residue
B	SER169
B	LYS289
B	D15600

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 1483

Chain	Residue
B	ASN365
B	GLU366
B	LYS393
D	ARG300

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 1483

Chain	Residue
C	LYS225
C	ARG226

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 1484

Chain	Residue
C	LYS264
C	ARG300
C	SER301

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1484

Chain	Residue
B	LYS264
B	ARG300
B	SER301

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 1485

Chain	Residue
B	HIS424
B	LYS453

site_id	CC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL D 1484

Chain	Residue
B	ARG325

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	68
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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	GLU291
A	ASP287

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP287
B	SER324
B	LYS289

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP287
C	SER324
C	LYS289

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP287
D	SER324
D	LYS289

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASN292
A	ASP287
A	LYS289

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASN292
B	ASP287
B	LYS289

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASN292
C	ASP287
C	LYS289

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASN292
D	ASP287
D	LYS289

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	GLU291
B	ASP287

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	GLU291
C	ASP287

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	GLU291
D	ASP287

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP287
A	LYS289

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP287
B	LYS289

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP287
C	LYS289

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP287
D	LYS289

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP287
A	SER324
A	LYS289

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