3fme

X-ray diffraction
2.26Å resolution

Crystal Structure of Human Mitogen-Activated Protein Kinase Kinase 6 (MEK6) Activated Mutant (S207D, T211D)

Released:
Source organism: Homo sapiens
Entry authors: Filippakopoulos P, Barr A, Pike ACW, Berridge G, Elkins J, Fedorov O, Keates T, Savitsky P, Soundararajan M, von Delft F, Arrowsmith CH, Edwards AM, Weigelt J, Bountra C, Knapp S, Structural Genomics Consortium (SGC)

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)
PDBe Complex ID:
PDB-CPX-156562 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity mitogen-activated protein kinase kinase 6 Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 32.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52564 (Residues: 47-334; Coverage: 86%)
Gene names: MAP2K6, MEK6, MKK6, PRKMK6, SKK3
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3121
Unit cell:
a: 132.756Å b: 132.756Å c: 45.719Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.212 0.236
Expression system: Escherichia coli