› 4qte

X-ray diffraction
1.5Å resolution

Structure of ERK2 in complex with VTX-11e, 4-{2-[(2-CHLORO-4-FLUOROPHENYL)AMINO]-5-METHYLPYRIMIDIN-4-YL}-N-[(1S)-1-(3-CHLOROPHENYL)-2-HYDROXYETHYL]-1H-PYRROLE-2-CARBOXAMIDE

Released:
DOI: 10.2210/pdb4qte/pdb
PDB entry 4qte coloured by chain, front view.
PDB entry 4qte coloured by chain, side view.
PDB entry 4qte coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics.
Chaikuad A, Tacconi EM, Zimmer J, Liang Y, Gray NS, Tarsounas M, Knapp S
Nat Chem Biol 10 853-60 (2014)
PMID: 25195011

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-151230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 361 amino acids
Theoretical weight: 41.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P28482 (Residues: 1-360; Coverage: 100%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand EDO 22 x EDO
Ligand SO4 5 x SO4
Ligand CL 2 x CL
Ligand 390 1 x 390
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 96.729Å b: 96.729Å c: 95.382Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.146 0.167
Expression system: Escherichia coli BL21

Quick links

Citations

20 review citations

Targeting RAS-ERK signalling in cancer: promises and challenges.
Samatar et al. (2014)
19 more

11 mentions without citation

A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics.
Chaikuad et al. (2014)
10 more