4YR8

Crystal structure of JNK in complex with a regulator protein

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	0006470	biological_process	protein dephosphorylation
B	0016311	biological_process	dephosphorylation
B	0017017	molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity
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	0006470	biological_process	protein dephosphorylation
D	0016311	biological_process	dephosphorylation
D	0017017	molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity
E	0004672	molecular_function	protein kinase activity
E	0004707	molecular_function	MAP kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0004707	molecular_function	MAP kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0006470	biological_process	protein dephosphorylation
G	0016311	biological_process	dephosphorylation
G	0017017	molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity
H	0006470	biological_process	protein dephosphorylation
H	0016311	biological_process	dephosphorylation
H	0017017	molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CL G 401

Chain	Residue
G	CYS244
G	HOH507

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site_id	AC2
Number of Residues	1
Details	binding site for residue CL B 401

Chain	Residue
B	ARG250

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site_id	AC3
Number of Residues	2
Details	binding site for residue CL D 401

Chain	Residue
D	CYS244
D	ARG250

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site_id	AC4
Number of Residues	2
Details	binding site for residue CL H 401

Chain	Residue
H	CYS244
H	ARG250

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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
E	ILE147-VAL159

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site_id	PS00383
Number of Residues	11
Details	TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. VHClaGisRSA

Chain	Residue	Details
G	VAL242-ALA252

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

Chain	Residue	Details
E	PHE61-CYS163

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160

Chain	Residue	Details
G	CYS244
B	CYS244
D	CYS244
H	CYS244

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
E	ILE32
E	LYS55
A	ILE32
A	LYS55
C	ILE32
C	LYS55
F	ILE32
F	LYS55

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P49185

Chain	Residue	Details
E	CYS116
A	CYS116
C	CYS116
F	CYS116

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site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:11062067

Chain	Residue	Details
E	THR183
A	THR183
C	THR183
F	THR183

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site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:11062067

Chain	Residue	Details
E	TYR185
A	TYR185
C	TYR185
F	TYR185

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