› 4qpa

X-ray diffraction
2.85Å resolution

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

Released:
DOI: 10.2210/pdb4qpa/pdb
PDB 4qpa coloured by chain and viewed from the front.
PDB 4qpa coloured by chain and viewed from the side.
PDB 4qpa coloured by chain and viewed from the top.
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. (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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 369 amino acids
Theoretical weight: 42.63 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 35W 2 x 35W
1 modified residue:
Ligand NEP 2 x NEP

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P41212
Unit cell:
a: 82.703Å b: 82.703Å c: 275.892Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.253
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

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

2 mentions without citation

Data-driven analysis and druggability assessment methods to accelerate the identification of novel cancer targets.
Beis et al. (2023)
1 more