› 7un4

X-ray diffraction
2.7Å resolution

Structure of MAP kinase phosphatase 5 in complex with 3,3-dimethyl-1-((9-propyl-5,6-dihydrothieno[3,4-h]quinazolin-2-yl)thio)butan-2-one, an allosteric inhibitor

Released:
DOI: 10.2210/pdb7un4/pdb
PDB entry 7un4 coloured by chain, front view.
PDB entry 7un4 coloured by chain, side view.
PDB entry 7un4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Defining the structure-activity relationship for a novel class of allosteric MKP5 inhibitors.
Gannam ZTK, Jamali H, Kweon OS, Herrington J, Shillingford SR, Papini C, Gentzel E, Lolis E, Bennett AM, Ellman JA, Anderson KS
Eur J Med Chem 243 114712 (2022)
PMID: 36116232

Function and Biology Details

Reactions catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 10 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 152 amino acids
Theoretical weight: 17.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y6W6 (Residues: 320-467; Coverage: 31%)
Gene names: DUSP10, MKP5
Sequence domains: Dual specificity phosphatase, catalytic domain

Ligands and Environments

1 bound ligand:
Ligand NVF 6 x NVF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 65.262Å b: 130.756Å c: 83.598Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.203 0.263
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

MKP1 promotes nonalcoholic steatohepatitis by suppressing AMPK activity through LKB1 nuclear retention.
Qiu et al. (2023)

1 mention without citation

Defining the structure-activity relationship for a novel class of allosteric MKP5 inhibitors.
Gannam et al. (2022)