› 5n65

X-ray diffraction
2Å resolution

Crystal Structure of p38alpha in Complex with Lipid Pocket Ligand 9h

Released:
DOI: 10.2210/pdb5n65/pdb
PDB 5n65 coloured by chain and viewed from the front.
PDB 5n65 coloured by chain and viewed from the side.
PDB 5n65 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structure-based design, synthesis and crystallization of 2-arylquinazolines as lipid pocket ligands of p38α MAPK.
Bührmann M, Wiedemann BM, Müller MP, Hardick J, Ecke M, Rauh D
OpenAccess logo PLoS One 12 e0184627 (2017)
PMID: 28892510

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: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 41.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16539 (Residues: 1-360; 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 8OT 2 x 8OT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 68.95Å b: 69.74Å c: 74.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.192 0.216
Expression system: Escherichia coli

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Citations

2 citation in other articles

Novel method to identify group-specific non-catalytic pockets of human kinome for drug design.
Wang et al. (2020)
1 more