PDBe 5ax3

X-ray diffraction
2.98Å resolution

Crystal structure of ERK2 complexed with allosteric and ATP-competitive inhibitors.

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 368 amino acids
Theoretical weight: 42.23 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:
Signal transducer and activator of transcription 3 Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.49 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P40763 (Residues: 571-582; Coverage: 2%)
Gene names: APRF, STAT3

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 43.835Å b: 66.465Å c: 116.871Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.236 0.285
Expression systems:
  • Escherichia coli BL21
  • Not provided