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2ZDU

Crystal Structure of human JNK3 complexed with an isoquinolone 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 Residues15
DetailsBINDING SITE FOR RESIDUE 446 A 901
ChainResidue
ALYS68
AALA151
AASN152
ASER193
AVAL196
ALEU206
AHOH918
AILE70
AGLY71
ASER72
AALA80
AALA91
AGLU147
ALEU148
AMET149

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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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