› 4qta

X-ray diffraction
1.45Å resolution

Structure of human ERK2 in complex with SCH772984 revealing a novel inhibitor-induced binding pocket

Released:
DOI: 10.2210/pdb4qta/pdb
PDB 4qta coloured by chain and viewed from the front.
PDB 4qta coloured by chain and viewed from the side.
PDB 4qta coloured by chain and viewed from the top.
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

Assembly composition:
monomeric (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

3 bound ligands:
Ligand EDO 8 x EDO
Ligand SO4 2 x SO4
Ligand 38Z 1 x 38Z
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 42.82Å b: 75.54Å c: 103.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.191
Expression system: Escherichia coli BL21

Quick links

Citations

18 review citations

A Perspective on the Development of c-Jun N-terminal Kinase Inhibitors as Therapeutics for Alzheimer's Disease: Investigating Structure through Docking Studies.
Cho et al. (2021)
17 more

15 mentions without citation

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