Structure of PDB 1pmv Chain A

Receptor sequence
>1pmvA (length=347) Species: 9606 (Homo sapiens) [Search protein sequence]
DNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKK
LSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYL
VMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN
IVVKSDCTLKILDFGLASFMMTPYVVTRYYRAPEVILGMGYKENVDIWSV
GCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVE
NRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRIS
VDDALQHPYINVWYDPAEVEAPPPQQLDEREHTIEEWKELIYKEVMN
3D structure
PDB1pmv The structure of JNK3 in complex with small molecule inhibitors: structural basis for potency and selectivity
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D189 K191 N194 D207 T226
Catalytic site (residue number reindexed from 1) D145 K147 N150 D163 T177
Enzyme Commision number 2.7.11.24: mitogen-activated protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 537 A I70 A91 M146 L148 M149 D150 A151 V196 L206 I26 A47 M102 L104 M105 D106 A107 V152 L162 MOAD: ic50=150nM
PDBbind-CN: -logKd/Ki=6.82,IC50=150nM
BindingDB: IC50=190nM,Kd=22nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004707 MAP kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1pmv, PDBe:1pmv, PDBj:1pmv
PDBsum1pmv
PubMed12954329
UniProtP53779|MK10_HUMAN Mitogen-activated protein kinase 10 (Gene Name=MAPK10)

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