1urh

X-ray diffraction
2.8Å resolution

The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-mercaptopyruvate sulfurtransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 30.74 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31142 (Residues: 2-281; Coverage: 100%)
Gene names: JW2505, b2521, sseA
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43
Unit cell:
a: 150.17Å b: 150.17Å c: 37.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.289
Expression system: Escherichia coli BL21(DE3)