› 4qp9

X-ray diffraction
2Å resolution

Crystal Structure of ERK2 in complex with 7-(1-propyl-1H-pyrazol-4-yl)-2-(pyridin-4-yl)-5H-pyrrolo[2,3-b]pyrazine

Released:
DOI: 10.2210/pdb4qp9/pdb
PDB entry 4qp9 coloured by chain, front view.
PDB entry 4qp9 coloured by chain, side view.
PDB entry 4qp9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Fragment-based discovery of potent ERK2 pyrrolopyrazine inhibitors.
Burdick DJ, Wang S, Heise C, Pan B, Drummond J, Yin J, Goeser L, Magnuson S, Blaney J, Moffat J, Wang W, Chen H
Bioorg Med Chem Lett 25 4728-4732 (2015)
PMID: 26338362

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)
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: 369 amino acids
Theoretical weight: 42.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28482 (Residues: 1-360; Coverage: 100%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 35X 1 x 35X
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 44.2Å b: 66.187Å c: 59.47Å
α: 90° β: 101.48° γ: 90°
R-values:
R R work R free
0.186 0.184 0.227
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Development of small molecule extracellular signal-regulated kinases (ERKs) inhibitors for cancer therapy.
Pan et al. (2022)
1 more

1 mention without citation

An automatic pipeline for the design of irreversible derivatives identifies a potent SARS-CoV-2 Mpro inhibitor.
Zaidman et al. (2021)