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3TTJ

Crystal Structure of JNK3 complexed with CC-359, a JNK inhibitor for the prevention of ischemia-reperfusion injury

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004705molecular_functionJUN kinase activity
A0004707molecular_functionMAP kinase activity
A0004708molecular_functionMAP kinase kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0007254biological_processJNK cascade
A0009416biological_processresponse to light stimulus
A0016020cellular_componentmembrane
A0016310biological_processphosphorylation
A0033554biological_processcellular response to stress
A0038095biological_processFc-epsilon receptor signaling pathway
A0042752biological_processregulation of circadian rhythm
A0048511biological_processrhythmic process
A0090398biological_processcellular senescence
A0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE JBI A 465
ChainResidue
AGLY71
AGLN155
AVAL196
ALEU206
AHOH495
AVAL78
AALA91
ALYS93
AILE124
AMET146
AGLU147
AMET149
AASN152

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpsNIVV
ChainResidueDetails
AILE185-VAL197

site_idPS01351
Number of Residues103
DetailsMAPK MAP kinase signature. FqnqthakrayRElvlmkcvnhkniisllnvftpqktleefqdvylvmelmdanlcqviqmeldhermsyllyqmlcgikhlhsagiih..........RDlKpsnivvksdC
ChainResidueDetails
APHE99-CYS201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP189

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AILE70
ALYS93

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAP2K7 => ECO:0000269|PubMed:10715136
ChainResidueDetails
ATHR221

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by MAP2K4 => ECO:0000269|PubMed:10715136
ChainResidueDetails
ATYR223

site_idSWS_FT_FI5
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:21941371
ChainResidueDetails
ACYS462
ACYS463

226707

PDB entries from 2024-10-30

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