› 1h4k

X-ray diffraction
2.05Å resolution

Sulfurtransferase from Azotobacter vinelandii in complex with hypophosphite

Released:
DOI: 10.2210/pdb1h4k/pdb
PDB entry 1h4k coloured by chain, front view.
PDB entry 1h4k coloured by chain, side view.
PDB entry 1h4k coloured by chain, top view.
Source organism: Azotobacter vinelandii
Primary publication:
A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese.
Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S
Biol Chem 382 1245-52 (2001)
PMID: 11592406

Function and Biology Details

Reaction catalysed: 
Thiosulfate + cyanide = sulfite + thiocyanate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156479 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiosulfate sulfurtransferase Chain: X
Molecule details ›
Chain: X
Length: 271 amino acids
Theoretical weight: 29.66 KDa
Source organism: Azotobacter vinelandii
Expression system: Escherichia coli M15
UniProt:
  • Canonical: P52197 (Residues: 1-271; Coverage: 100%)
Gene name: rhdA
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

3 bound ligands:
Ligand PO2 1 x PO2
Ligand SO4 2 x SO4
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 40.295Å b: 151.465Å c: 53.638Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.24
Expression system: Escherichia coli M15

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Citations

16 citation in other articles

Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation.
Tamura et al. (2004)
15 more

2 mentions without citation

Involvement of the Azotobacter vinelandii rhodanese-like protein RhdA in the glutathione regeneration pathway.
Remelli et al. (2012)
1 more