PDBe 2zoq

X-ray diffraction
2.39Å resolution

Structural dissection of human mitogen-activated kinase ERK1

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human mono-phosphorylated ERK1 at Tyr204.
Biochem. Biophys. Res. Commun. 377 1123-7 (2008)
PMID: 18983981

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 382 amino acids
Theoretical weight: 43.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P27361 (Residues: 1-379; Coverage: 100%)
Gene names: ERK1, MAPK3, PRKM3
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 62.382Å b: 91.54Å c: 64.93Å
α: 90° β: 91.5° γ: 90°
R-values:
R R work R free
0.249 0.249 0.267
Expression system: Escherichia coli