› 2fst

X-ray diffraction
1.45Å resolution

mitogen activated protein kinase p38alpha (D176A+F327L) activating mutant

Released:
DOI: 10.2210/pdb2fst/pdb
PDB 2fst coloured by chain and viewed from the front.
PDB 2fst coloured by chain and viewed from the side.
PDB 2fst coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structures of p38alpha active mutants reveal conformational changes in L16 loop that induce autophosphorylation and activation.
Diskin R, Lebendiker M, Engelberg D, Livnah O
J. Mol. Biol. 365 66-76 (2007)
PMID: 17059827

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 14 Chain: X
Molecule details ›
Chain: X
Length: 367 amino acids
Theoretical weight: 42.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16539 (Residues: 2-360; Coverage: 100%)
Gene names: CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2, SAPK2A
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand BOG 3 x BOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 68.673Å b: 69.786Å c: 74.227Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.206 0.241
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Atypical p38 Signaling, Activation, and Implications for Disease.
Burton et al. (2021)
5 more

4 mentions without citation

Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38alpha MAP kinase.
Sours et al. (2008)
3 more