Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A2C

Crystal structure of a pyrazolopyrimidine inhibitor complex bound to MAPKAP Kinase-2 (MK2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation
I	0004672	molecular_function	protein kinase activity
I	0005524	molecular_function	ATP binding
I	0006468	biological_process	protein phosphorylation
J	0004672	molecular_function	protein kinase activity
J	0005524	molecular_function	ATP binding
J	0006468	biological_process	protein phosphorylation
K	0004672	molecular_function	protein kinase activity
K	0005524	molecular_function	ATP binding
K	0006468	biological_process	protein phosphorylation
L	0004672	molecular_function	protein kinase activity
L	0005524	molecular_function	ATP binding
L	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PDY A 1

Chain	Residue
A	GLN80
A	LEU193
A	ASP207
A	ALA91
A	VAL118
A	GLU139
A	CYS140
A	LEU141
A	ASP142
A	GLU190
A	ASN191

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PDY A 2

Chain	Residue
A	TYR260
A	PRO261
A	TYR264

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PDY B 1

Chain	Residue
B	VAL78
B	GLN80
B	ALA91
B	GLU139
B	CYS140
B	LEU141
B	GLU190
B	ASN191
B	ASP207

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PDY B 2

Chain	Residue
B	TYR260
B	PRO261
B	TYR264
B	SER265
E	PRO199
E	ASN200

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PDY C 1

Chain	Residue
C	VAL78
C	GLN80
C	ALA91
C	VAL118
C	MET138
C	GLU139
C	CYS140
C	LEU141
C	ASP142
C	GLU190
C	ASN191
C	THR206
C	ASP207

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PDY C 2

Chain	Residue
C	TYR260
C	PRO261
C	TYR264
C	SER265

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PDY D 1

Chain	Residue
D	VAL78
D	GLN80
D	ALA91
D	VAL118
D	MET138
D	GLU139
D	CYS140
D	LEU141
D	GLU190
D	ASN191
D	LEU193
D	ASP207

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PDY D 2

Chain	Residue
D	PHE147
D	TYR264

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PDY E 1

Chain	Residue
E	VAL78
E	GLN80
E	ALA91
E	VAL118
E	GLU139
E	CYS140
E	LEU141
E	GLU190
E	ASN191
E	LEU193
E	ASP207

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PDY E 2

Chain	Residue
E	TYR260
E	PRO261
E	TYR264

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDY F 1

Chain	Residue
F	VAL78
F	GLN80
F	ALA91
F	VAL118
F	GLU139
F	CYS140
F	LEU141
F	GLU190
F	ASN191
F	ASP207

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PDY F 2

Chain	Residue
A	PRO199
F	TYR260
F	PRO261
F	TYR264
F	SER265
F	LEU269

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PDY G 1

Chain	Residue
G	ASN191
G	LEU193
G	THR206
G	ASP207
G	VAL78
G	GLN80
G	ALA91
G	VAL118
G	GLU139
G	CYS140
G	LEU141
G	ASP142
G	GLU190

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PDY G 2

Chain	Residue
G	TYR260
G	PRO261
G	TYR264
G	SER265

site_id	BC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PDY H 1

Chain	Residue
H	VAL78
H	GLN80
H	ALA91
H	VAL118
H	MET138
H	GLU139
H	CYS140
H	LEU141
H	GLU190
H	ASN191
H	LEU193
H	THR206
H	ASP207

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PDY H 2

Chain	Residue
G	TYR229
H	PRO261
H	TYR264
H	SER265

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDY I 1

Chain	Residue
I	ALA91
I	VAL118
I	GLU139
I	CYS140
I	LEU141
I	GLU190
I	ASN191
I	LEU193
I	THR206
I	ASP207

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PDY I 2

Chain	Residue
I	PHE147
I	PRO261
I	TYR264
I	SER265

site_id	CC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PDY J 1

Chain	Residue
J	VAL78
J	GLN80
J	ALA91
J	VAL118
J	MET138
J	GLU139
J	CYS140
J	LEU141
J	GLU190
J	ASN191
J	LEU193
J	ASP207

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PDY J 2

Chain	Residue
J	TYR260
J	PRO261
J	TYR264
J	SER265

site_id	CC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDY K 1

Chain	Residue
K	VAL78
K	GLN80
K	ALA91
K	VAL118
K	GLU139
K	CYS140
K	LEU141
K	GLU190
K	ASN191
K	ASP207

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PDY K 2

Chain	Residue
K	PHE147
K	TYR260
K	PRO261
K	TYR264

site_id	CC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PDY L 1

Chain	Residue
L	VAL78
L	GLN80
L	ALA91
L	GLU139
L	CYS140
L	LEU141
L	ASP142
L	GLU190
L	ASN191
L	THR206
L	ASP207

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PDY L 2

Chain	Residue
L	PRO261
L	TYR264
L	SER265

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 3

Chain	Residue
F	SER265
F	ASN266
F	SER272
F	GLY274
F	ARG278

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK

Chain	Residue	Details
A	LEU70-LYS93

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY

Chain	Residue	Details
A	ILE182-TYR194

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP186
J	ASP186
K	ASP186
L	ASP186
B	ASP186
C	ASP186
D	ASP186
E	ASP186
F	ASP186
G	ASP186
H	ASP186
I	ASP186

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU70
E	LYS93
F	LEU70
F	LYS93
G	LEU70
G	LYS93
H	LEU70
H	LYS93
I	LEU70
I	LYS93
J	LEU70
A	LYS93
J	LYS93
K	LEU70
K	LYS93
L	LEU70
L	LYS93
B	LEU70
B	LYS93
C	LEU70
C	LYS93
D	LEU70
D	LYS93
E	LEU70

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	GLU139
J	GLU139
K	GLU139
L	GLU139
B	GLU139
C	GLU139
D	GLU139
E	GLU139
F	GLU139
G	GLU139
H	GLU139
I	GLU139

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphothreonine; by MAPK14 => ECO:0000269\|PubMed:8846784

Chain	Residue	Details
A	THR222
J	THR222
K	THR222
L	THR222
B	THR222
C	THR222
D	THR222
E	THR222
F	THR222
G	THR222
H	THR222
I	THR222

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine; by MAPK14 => ECO:0000269\|PubMed:8846784

Chain	Residue	Details
A	SER272
J	SER272
K	SER272
L	SER272
B	SER272
C	SER272
D	SER272
E	SER272
F	SER272
G	SER272
H	SER272
I	SER272

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250

Chain	Residue	Details
A	SER328
J	SER328
K	SER328
L	SER328
B	SER328
C	SER328
D	SER328
E	SER328
F	SER328
G	SER328
H	SER328
I	SER328

site_id	SWS_FT_FI7
Number of Residues	12
Details	MOD_RES: Phosphothreonine; by MAPK14 => ECO:0000269\|PubMed:8846784, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	THR334
J	THR334
K	THR334
L	THR334
B	THR334
C	THR334
D	THR334
E	THR334
F	THR334
G	THR334
H	THR334
I	THR334

site_id	SWS_FT_FI8
Number of Residues	24
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269\|PubMed:21131586

Chain	Residue	Details
A	LYS353
F	LYS353
G	LYS353
H	LYS353
I	LYS353
J	LYS353
K	LYS353
L	LYS353
B	LYS353
C	LYS353
D	LYS353
E	LYS353

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