PDBe 4h3p

X-ray diffraction
2.3Å resolution

Crystal structure of human ERK2 complexed with a MAPK docking peptide

Released:
Source organism: Homo sapiens
Primary publication:
Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 69 486-9 (2013)
PMID: 23519423

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitogen-activated protein kinase 1 Chains: A, D
Molecule details ›
Chains: A, D
Length: 362 amino acids
Theoretical weight: 41.44 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:
Ribosomal protein S6 kinase alpha-1 Chains: B, E
Molecule details ›
Chains: B, E
Length: 24 amino acids
Theoretical weight: 2.66 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15418 (Residues: 712-735; Coverage: 3%)
Gene names: MAPKAPK1A, RPS6KA1, RSK1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 41.48Å b: 58.77Å c: 79.18Å
α: 100.93° β: 98.96° γ: 90.01°
R-values:
R R work R free
0.18 0.178 0.224
Expression systems:
  • Escherichia coli
  • Not provided