› 1ilw

X-ray diffraction
2.05Å resolution

Crystal Structure of Pyrazinamidase/Nicotinamidase of Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb1ilw/pdb
PDB entry 1ilw coloured by chain, front view.
PDB entry 1ilw coloured by chain, side view.
PDB entry 1ilw coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii.
Du X, Wang W, Kim R, Yakota H, Nguyen H, Kim SH
Biochemistry 40 14166-72 (2001)
PMID: 11714269

Function and Biology Details

Reaction catalysed: 
Nicotinamide + H(2)O = nicotinate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129760 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
nicotinamidase Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 20.22 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58727 (Residues: 1-180; Coverage: 100%)
Gene name: PH0999
Sequence domains: Isochorismatase family
Structure domains: Isochorismatase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 32.977Å b: 43.418Å c: 55.781Å
α: 90° β: 101.22° γ: 90°
R-values:
R R work R free
0.189 0.181 0.257
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Protein acetylation in metabolism - metabolites and cofactors.
Menzies et al. (2016)
4 more

6 mentions without citation

Beyond antibody engineering: directed evolution of alternative binding scaffolds and enzymes using yeast surface display.
Könning et al. (2018)
5 more