Structure of PDB 4y5h Chain A

Receptor sequence
>4y5hA (length=349) Species: 9606 (Homo sapiens) [Search protein sequence]
DNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKK
LSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYL
VMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN
IVVKSDCTLKILDFGLARTASFMMTPYVVTRYYRAPEVILGMGYKENVDI
WSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRN
YVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAK
RISVDDALQHPYINVWYDPAEVEAPPPQLDEREHTIEEWKELIYKEVMN
3D structure
PDB4y5h Pyridopyrimidinone Derivatives as Potent and Selective c-Jun N-Terminal Kinase (JNK) Inhibitors.
ChainA
Resolution2.055 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 T180
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 519 A I70 A91 M146 M149 Q155 L206 I26 A47 M102 M105 Q111 L162 MOAD: ic50=15nM
PDBbind-CN: -logKd/Ki=7.82,IC50=15nM
BindingDB: IC50=15nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004707 MAP kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:4y5h, PDBe:4y5h, PDBj:4y5h
PDBsum4y5h
PubMed25893042
UniProtP53779|MK10_HUMAN Mitogen-activated protein kinase 10 (Gene Name=MAPK10)

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