› 5wqj

X-ray diffraction
1.2Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) 2-oxo-3-sulfanylpropanoate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine = pyruvate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-mercaptopyruvate sulfurtransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 297 amino acids
Theoretical weight: 33.07 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99J99 (Residues: 1-297; Coverage: 100%)
Gene name: Mpst
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

2 bound ligands:
Ligand 7N3 2 x 7N3
Ligand NA 5 x NA
1 modified residue:
Ligand CSS 2 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 37.355Å b: 150.36Å c: 54.307Å
α: 90° β: 110.09° γ: 90°
R-values:
R R work R free
0.141 0.14 0.171
Expression system: Escherichia coli

Quick links

Citations

20 review citations

International Union of Basic and Clinical Pharmacology. CII: Pharmacological Modulation of H2S Levels: H2S Donors and H2S Biosynthesis Inhibitors.
Szabo et al. (2017)
19 more

1 mention without citation

Discovery and Mechanistic Characterization of Selective Inhibitors of H2S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine Persulfide.
Hanaoka et al. (2017)