6EMH

Crystal structure of JNK3 in complex with a pyridinylimidazole inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004707	molecular_function	MAP kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004707	molecular_function	MAP kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004707	molecular_function	MAP kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004707	molecular_function	MAP kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue BME A 501

Chain	Residue
A	LYS198
A	SER199
A	CYS201
A	HOH681

---

site_id	AC2
Number of Residues	6
Details	binding site for residue BME A 502

Chain	Residue
A	HOH765
A	CYS154
A	PRO192
A	TYR229
A	GLU255
A	HOH757

---

site_id	AC3
Number of Residues	3
Details	binding site for residue CL A 503

Chain	Residue
A	LYS62
A	ARG63
A	HOH672

---

site_id	AC4
Number of Residues	10
Details	binding site for residue BGE A 504

Chain	Residue
A	VAL78
A	ALA91
A	MET146
A	GLU147
A	MET149
A	ASP150
A	ASN152
A	LEU206
A	HOH710
A	HOH726

---

site_id	AC5
Number of Residues	1
Details	binding site for residue EDO A 505

Chain	Residue
A	GLU164

---

site_id	AC6
Number of Residues	11
Details	binding site for residue C15 A 506

Chain	Residue
A	GLY215
A	THR216
A	ILE235
A	LEU236
A	GLY237
A	GLY239
A	ILE269
A	GLN291
A	HOH610
C	GLU160
C	ARG165

---

site_id	AC7
Number of Residues	11
Details	binding site for residue BGE B 502

Chain	Residue
B	VAL78
B	ALA91
B	MET146
B	GLU147
B	MET149
B	ASP150
B	ALA151
B	ASN152
B	LEU206
B	HOH702
B	HOH745

---

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO B 503

Chain	Residue
B	GLU164
B	ASP200

---

site_id	AC9
Number of Residues	9
Details	binding site for residue C15 B 504

Chain	Residue
B	GLY215
B	THR216
B	ILE235
B	GLY237
B	GLY239
B	GLN291
D	GLU160
D	ASP162
D	ARG165

---

site_id	AD1
Number of Residues	6
Details	binding site for residue CL C 501

Chain	Residue
A	HOH682
C	GLU242
C	ASN243
C	SER349
C	VAL350
C	HOH633

---

site_id	AD2
Number of Residues	2
Details	binding site for residue PEG C 502

Chain	Residue
C	CYS201
C	HOH693

---

site_id	AD3
Number of Residues	9
Details	binding site for residue BGE C 503

Chain	Residue
C	VAL78
C	ALA91
C	MET146
C	GLU147
C	MET149
C	GLN155
C	LEU206
C	HOH730
C	HOH740

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO C 504

Chain	Residue
B	TYR168
C	GLN100
C	ASN101

---

site_id	AD5
Number of Residues	6
Details	binding site for residue GOL C 505

Chain	Residue
A	HIS259
C	PRO344
C	ALA345
C	LYS346
C	ARG347
C	HOH638

---

site_id	AD6
Number of Residues	5
Details	binding site for residue CL D 501

Chain	Residue
D	GLU242
D	ASN243
D	SER349
D	VAL350
D	HOH618

---

site_id	AD7
Number of Residues	2
Details	binding site for residue PEG D 502

Chain	Residue
D	VAL197
D	CYS201

---

site_id	AD8
Number of Residues	9
Details	binding site for residue BGE D 503

Chain	Residue
D	ILE70
D	MET146
D	GLU147
D	MET149
D	ALA151
D	ASN152
D	GLN155
D	LEU206
D	HOH694

---

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO D 504

Chain	Residue
D	LYS178
D	HOH669

---

site_id	AE1
Number of Residues	4
Details	binding site for residue EDO D 505

Chain	Residue
A	TYR168
A	TRP362
D	GLN100
D	ASN101

---

site_id	AE2
Number of Residues	5
Details	binding site for residue GOL D 506

Chain	Residue
D	PRO344
D	ALA345
D	ARG347
D	HOH645
D	HOH666

---

site_id	AE3
Number of Residues	5
Details	binding site for residue GOL D 507

Chain	Residue
C	ARG227
C	ARG266
C	HOH647
D	ASN296
D	ASN300

---

site_id	AE4
Number of Residues	10
Details	binding site for Di-peptide BME B 501 and CYS B 201

Chain	Residue
B	MET159
B	TYR168
B	LEU169
B	GLN172
B	VAL197
B	LYS198
B	SER199
B	ASP200
B	THR202
B	LEU203

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE185-VAL197

---

site_id	PS01351
Number of Residues	103
Details	MAPK MAP kinase signature. FqnqthakrayRElvlmkcvnhkniisllnvftpqktleefqdvylvmelmdanlcqviqmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC

Chain	Residue	Details
A	PHE99-CYS201

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP189
B	ASP189
C	ASP189
D	ASP189

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	ILE70
A	LYS93
B	ILE70
B	LYS93
C	ILE70
C	LYS93
D	ILE70
D	LYS93

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:10715136

Chain	Residue	Details
A	THR221
B	THR221
C	THR221
D	THR221

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:10715136

Chain	Residue	Details
A	TYR223
B	TYR223
C	TYR223
D	TYR223

---