› 6d5y

X-ray diffraction
2.86Å resolution

Crystal structure of ERK2 G169D mutant

Released:
DOI: 10.2210/pdb6d5y/pdb
PDB entry 6d5y coloured by chain, front view.
PDB entry 6d5y coloured by chain, side view.
PDB entry 6d5y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ERK Mutations and Amplification Confer Resistance to ERK-Inhibitor Therapy.
Jaiswal BS, Durinck S, Stawiski EW, Yin J, Wang W, Lin E, Moffat J, Martin SE, Modrusan Z, Seshagiri S
Clin Cancer Res 24 4044-4055 (2018)
PMID: 29760222

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: 348 amino acids
Theoretical weight: 40.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28482 (Residues: 13-360; Coverage: 97%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 44.87Å b: 65.4Å c: 116.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.272
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Targeting Alterations in the RAF-MEK Pathway.
Yaeger et al. (2019)
11 more