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3O2M

Crystal Structure of JNK1-alpha1 isoform complex with a biaryl tetrazol (A-82118)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004707molecular_functionMAP kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004707molecular_functionMAP kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 46A A 701
ChainResidue
APHE180
BPRO184
BTHR255
B46A701
AILE197
ALEU198
AGLY199
ATYR230
AILE231
AGLN253
ATHR255
AVAL256

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 46A B 701
ChainResidue
APRO184
AVAL256
A46A701
BPHE180
BILE197
BGLY199
BTYR230
BILE231
BGLN253
BTHR255
BVAL256

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AARG189
AARG192
ATYR230
BTHR255
BASN258

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
ALYS68
AARG69
AARG72
AARG150
AMET181

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 801
ChainResidue
ATHR255
BARG189
BARG192
BTYR230

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BLYS68
BARG69
BARG72
BARG150
BARG174
BMET181

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpsNIVV
ChainResidueDetails
AILE147-VAL159

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FqnqthakrayRElvlmkcvnhkniigllnvftpqksleefqdvyivmelmdanlcqviqmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC
ChainResidueDetails
APHE61-CYS163

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP151
BASP151

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE32
BLYS55
AILE32
ALYS55

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P49185
ChainResidueDetails
ACYS116
BCYS116

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:11062067
ChainResidueDetails
AGLU183
BGLU183

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:11062067
ChainResidueDetails
AGLU185
BGLU185

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PDB entries from 2024-05-29

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