› 3s2s

X-ray diffraction
1.7Å resolution

The crystal structure of pyrazinamidase/nicotinamidase from streptococcus mutans UA159

Released:
DOI: 10.2210/pdb3s2s/pdb
PDB entry 3s2s coloured by chain, front view.
PDB entry 3s2s coloured by chain, side view.
PDB entry 3s2s coloured by chain, top view.
Source organism: Streptococcus mutans
Primary publication:
Get phases from arsenic anomalous scattering: de novo SAD phasing of two protein structures crystallized in cacodylate buffer.
Liu X, Zhang H, Wang XJ, Li LF, Su XD
OpenAccess logo PLoS One 6 e24227 (2011)
PMID: 21912678

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184178 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isochorismatase-like domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 217 amino acids
Theoretical weight: 24.09 KDa
Source organism: Streptococcus mutans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8DSG2 (Residues: 1-183; Coverage: 100%)
Gene names: SMU_1823, pncA
Sequence domains: Isochorismatase family
Structure domains: Isochorismatase-like

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand CAD 4 x CAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 76.49Å b: 80.12Å c: 130.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.191
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Small Molecule Active Site Directed Tools for Studying Human Caspases.
Poreba et al. (2015)
13 other articles

3 mentions without citation

Get phases from arsenic anomalous scattering: de novo SAD phasing of two protein structures crystallized in cacodylate buffer.
Liu et al. (2011)
2 more