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1PMV

The structure of JNK3 in complex with a dihydroanthrapyrazole inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004707molecular_functionMAP kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 537 A 501
ChainResidue
AILE70
AALA91
AMET146
AGLU147
ALEU148
AMET149
AASP150
AALA151
ALEU206

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP189
ASER193

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP189
ALYS191

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR226
AASP189
ALYS191

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP189
ALYS191
AASN194

222415

PDB entries from 2024-07-10

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