Structure of PDB 4h39 Chain A

Receptor sequence
>4h39A (length=340) Species: 9606 (Homo sapiens) [Search protein sequence]
DNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKK
LSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYL
VMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN
IVVKSDCTLKILDFGTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGE
MVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYA
GLTFPKLFPDSLFPNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYIN
VWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMN
3D structure
PDB4h39 Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases.
ChainA
Resolution1.992 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) D145 K147 N150 D163 T171
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 peptide A M159 R165 Y168 S199 D200 C201 W362 E367 M115 R121 Y124 S155 D156 C157 W302 E307
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:4h39, PDBe:4h39, PDBj:4h39
PDBsum4h39
PubMed23142346
UniProtP53779|MK10_HUMAN Mitogen-activated protein kinase 10 (Gene Name=MAPK10)

[Back to BioLiP]