› 1d0s

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF NICOTINATE MONONUCLEOTIDE : 5,6-DIMETHYLBENZIMIDAZOLE PHOSPHORIBOSYLTRANSFERASE (COBT) FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH 5, 6-DIMETHYLBENZIMIDAZOLE

Released:
DOI: 10.2210/pdb1d0s/pdb
PDB entry 1d0s coloured by chain, front view.
PDB entry 1d0s coloured by chain, side view.
PDB entry 1d0s coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
The three-dimensional structures of nicotinate mononucleotide:5,6- dimethylbenzimidazole phosphoribosyltransferase (CobT) from Salmonella typhimurium complexed with 5,6-dimethybenzimidazole and its reaction products determined to 1.9 A resolution.
Cheong CG, Escalante-Semerena JC, Rayment I
Biochemistry 38 16125-35 (1999)
PMID: 10587435

Function and Biology Details

Reaction catalysed: 
Beta-nicotinate D-ribonucleotide + 5,6-dimethylbenzimidazole = nicotinate + alpha-ribazole 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 356 amino acids
Theoretical weight: 36.65 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
UniProt:
  • Canonical: Q05603 (Residues: 1-356; Coverage: 100%)
Gene names: STM2016, cobT
Sequence domains: Phosphoribosyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 1 x PO4
Ligand DMD 1 x DMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 72.1Å b: 90.2Å c: 47.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 not available

Quick links

Citations

4 review citations

Structural analyses reveal two distinct families of nucleoside phosphorylases.
Pugmire et al. (2002)
3 more

3 mentions without citation

ResBoost: characterizing and predicting catalytic residues in enzymes.
Alterovitz et al. (2009)
2 more