4an2

X-ray diffraction
2.5Å resolution

Crystal structures of human MEK1 with carboxamide-based allosteric inhibitor XL518 (GDC-0973), or related analogs.

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity mitogen-activated protein kinase kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 301 amino acids
Theoretical weight: 33.61 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q02750 (Residues: 61-392; Coverage: 74%)
Gene names: MAP2K1, MEK1, PRKMK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P61
Unit cell:
a: 108.844Å b: 108.844Å c: 47.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.211 0.299
Expression system: Spodoptera frugiperda