› 1gol

X-ray diffraction
2.8Å resolution

COORDINATES OF RAT MAP KINASE ERK2 WITH AN ARGININE MUTATION AT POSITION 52

Released:
DOI: 10.2210/pdb1gol/pdb
PDB entry 1gol coloured by chain, front view.
PDB entry 1gol coloured by chain, side view.
PDB entry 1gol coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5'-triphosphate.
Robinson MJ, Harkins PC, Zhang J, Baer R, Haycock JW, Cobb MH, Goldsmith EJ
Biochemistry 35 5641-6 (1996)
PMID: 8639522

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 42.19 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63086 (Residues: 1-358; Coverage: 100%)
Gene names: Erk2, Mapk, Mapk1, Prkm1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 49.32Å b: 71.42Å c: 61.25Å
α: 90° β: 109.75° γ: 90°
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Synthesis and function of 3-phosphorylated inositol lipids.
Vanhaesebroeck et al. (2001)
10 more

7 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
6 more