› 6yg6

X-ray diffraction
2.15Å resolution

Crystal structure of MKK7 (MAP2K7) covalently bound with type-II inhibitor TL10-105

Released:
DOI: 10.2210/pdb6yg6/pdb
PDB entry 6yg6 coloured by chain, front view.
PDB entry 6yg6 coloured by chain, side view.
PDB entry 6yg6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic Domain Plasticity of MKK7 Reveals Structural Mechanisms of Allosteric Activation and Diverse Targeting Opportunities.
Schröder M, Tan L, Wang J, Liang Y, Gray NS, Knapp S, Chaikuad A
Cell Chem Biol 27 1285-1295.e4 (2020)
PMID: 32783966

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity mitogen-activated protein kinase kinase 7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 307 amino acids
Theoretical weight: 34.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O14733 (Residues: 100-405; Coverage: 73%)
Gene names: JNKK2, MAP2K7, MEK7, MKK7, PRKMK7, SKK4
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:
Ligand EDO 4 x EDO
Ligand OQ8 2 x OQ8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 72.651Å b: 69.934Å c: 73.763Å
α: 90° β: 119.36° γ: 90°
R-values:
R R work R free
0.205 0.204 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 citation in other articles

Reactivities of the Front Pocket N-Terminal Cap Cysteines in Human Kinases.
Liu et al. (2022)
9 more