Structure of PDB 6emh Chain D

Receptor sequence
>6emhD (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
NQFYSVEVGDSTFTVLKRYQNLKPIGIVCAAYDAVLDRNVAIKKLSRPFQ
NQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMD
ANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSD
CTLKILDFGLARTATRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKI
LFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPK
LFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINV
WYDPAEVEAPPPQIEHTIEEWKELIYKEVMN
3D structure
PDB6emh Structural Optimization of a Pyridinylimidazole Scaffold: Shifting the Selectivity from p38 alpha Mitogen-Activated Protein Kinase to c-Jun N-Terminal Kinase 3.
ChainD
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D189 K191 N194 D207 T226
Catalytic site (residue number reindexed from 1) D139 K141 N144 D157 T165
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 BGE D I70 M146 M149 A151 Q155 L206 I25 M96 M99 A101 Q105 L156 MOAD: ic50=833nM
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

View graph for
Biological Process
External links
PDB RCSB:6emh, PDBe:6emh, PDBj:6emh
PDBsum6emh
PubMed30087925
UniProtP53779|MK10_HUMAN Mitogen-activated protein kinase 10 (Gene Name=MAPK10)

[Back to BioLiP]