› 3vn9

X-ray diffraction
2.6Å resolution

Rifined Crystal structure of non-phosphorylated MAP2K6 in a putative auto-inhibition state

Released:
DOI: 10.2210/pdb3vn9/pdb
PDB entry 3vn9 coloured by chain, front view.
PDB entry 3vn9 coloured by chain, side view.
PDB entry 3vn9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of non-phosphorylated MAP2K6 in a putative auto-inhibition state.
Matsumoto T, Kinoshita T, Matsuzaka H, Nakai R, Kirii Y, Yokota K, Tada T
J Biochem 151 541-9 (2012)
PMID: 22383536

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

Assembly composition:
monomeric (preferred)
Assembly name:
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: 340 amino acids
Theoretical weight: 38.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52564 (Residues: 1-334; Coverage: 100%)
Gene names: MAP2K6, MEK6, MKK6, PRKMK6, SKK3
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P3121
Unit cell:
a: 83.456Å b: 83.456Å c: 101.153Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.265 0.264 0.28
Expression system: Escherichia coli

Quick links

Citations

1 review citation

JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships.
Zeke et al. (2016)
8 other articles

12 mentions without citation

The structural pathway of interleukin 1 (IL-1) initiated signaling reveals mechanisms of oncogenic mutations and SNPs in inflammation and cancer.
Acuner Ozbabacan et al. (2014)
11 more