Structure of PDB 3vuk Chain A

Receptor sequence
>3vukA (length=355) Species: 9606 (Homo sapiens) [Search protein sequence]
DNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKK
LSRPFQNQTHAKRAYRELVLMKVVNHKNIIGLLNVFTPQKSLEEFQDVYI
VMELMDANLSQVIQMELDHERMSYLLYQMLVGIKHLHSAGIIHRDLKPSN
IVVKSDATLKILDFGLARTAGTSTPYVVTRYYRAPEVILGMGYKENVDIW
SVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPSPEFMKKLQPTVRTY
VENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKR
ISVDEALQHPYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKE
VMDLE
3D structure
PDB3vuk Seven cysteine-deficient mutants depict the interplay between thermal and chemical stabilities of individual cysteine residues in mitogen-activated protein kinase c-Jun N-terminal kinase 1
ChainA
Resolution2.95 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) D151 K153 N156 D169 T188
Catalytic site (residue number reindexed from 1) D145 K147 N150 D163 T179
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 M121 R127 Y130 S161 D162 A163 W324 E329 M115 R121 Y124 S155 D156 A157 W315 E320
BS02 SO4 A R189 R192 H230 R180 R183 H221
BS03 SO4 A R69 R72 R150 R174 R63 R66 R144 R168
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:3vuk, PDBe:3vuk, PDBj:3vuk
PDBsum3vuk
PubMed23020677
UniProtP45983|MK08_HUMAN Mitogen-activated protein kinase 8 (Gene Name=MAPK8)

[Back to BioLiP]