› 1orb

X-ray diffraction
2Å resolution

ACTIVE SITE STRUCTURAL FEATURES FOR CHEMICALLY MODIFIED FORMS OF RHODANESE

Released:
DOI: 10.2210/pdb1orb/pdb
PDB entry 1orb coloured by chain, front view.
PDB entry 1orb coloured by chain, side view.
PDB entry 1orb coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Active site structural features for chemically modified forms of rhodanese.
Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R
J Biol Chem 271 21054-61 (1996)
PMID: 8702871

Function and Biology Details

Reaction catalysed: 
Thiosulfate + cyanide = sulfite + thiocyanate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiosulfate sulfurtransferase Chain: A
Molecule details ›
Chain: A
Length: 296 amino acids
Theoretical weight: 33.21 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00586 (Residues: 2-297; Coverage: 100%)
Gene name: TST
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 156.23Å b: 49.04Å c: 42.25Å
α: 90° β: 98.6° γ: 90°
R-values:
R R work R free
0.187 not available not available

Quick links

Citations

5 review citations

Chemical foundations of hydrogen sulfide biology.
Li et al. (2013)
4 more

1 mention without citation

Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
Koike et al. (2009)