› 3eqf

X-ray diffraction
2.7Å resolution

X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with K252A and MG2P

Released:
DOI: 10.2210/pdb3eqf/pdb
PDB entry 3eqf coloured by chain, front view.
PDB entry 3eqf coloured by chain, side view.
PDB entry 3eqf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of MEK1 binary and ternary complexes with nucleotides and inhibitors.
Fischmann TO, Smith CK, Mayhood TW, Myers JE, Reichert P, Mannarino A, Carr D, Zhu H, Wong J, Yang RS, Le HV, Madison VS
Biochemistry 48 2661-74 (2009)
PMID: 19161339

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:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-169744 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity mitogen-activated protein kinase kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 40.11 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q02750 (Residues: 35-393; Coverage: 91%)
Gene names: MAP2K1, MEK1, PRKMK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand KSA 1 x KSA
Ligand MG 1 x MG
Ligand CA 1 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P6122
Unit cell:
a: 78.16Å b: 78.16Å c: 222.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.257 0.254 not available
Expression system: Not provided

Quick links

Citations

30 review citations

MEK1 and MEK2 inhibitors and cancer therapy: the long and winding road.
Caunt et al. (2015)
29 more

10 mentions without citation

Kinase Atlas: Druggability Analysis of Potential Allosteric Sites in Kinases.
Yueh et al. (2019)
9 more