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1PMU

The crystal structure of JNK3 in complex with a phenantroline 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 Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1001
ChainResidue
ACYS283
AASP343
ALYS346

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 9HP A 501
ChainResidue
AMET149
AGLN155
ALEU206
AGLY73
AGLN75
AVAL78
AALA91
AGLU147
ALEU148

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

218853

PDB entries from 2024-04-24

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