5ktm

X-ray diffraction
1.44Å resolution

Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with a bound Fe4S4 cluster

Released:

Function and Biology Details

Reaction catalysed:
Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Quinolinate synthase Chain: A
Molecule details ›
Chain: A
Length: 304 amino acids
Theoretical weight: 34.58 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O57767 (Residues: 1-300; Coverage: 100%)
Gene names: PH0013, nadA
Sequence domains: Quinolinate synthetase A protein
Structure domains: NadA-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 47.48Å b: 52.877Å c: 55.996Å
α: 90° β: 111.72° γ: 90°
R-values:
R R work R free
0.173 0.171 0.215
Expression system: Escherichia coli BL21(DE3)