› 5ktr

X-ray diffraction
1.34Å resolution

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

Released:
DOI: 10.2210/pdb5ktr/pdb
PDB entry 5ktr coloured by chain, front view.
PDB entry 5ktr coloured by chain, side view.
PDB entry 5ktr coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.
Fenwick MK, Ealick SE
Biochemistry 55 4135-9 (2016)
PMID: 27404889

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129606 (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

4 bound ligands:
Ligand SF4 1 x SF4
Ligand MAE 1 x MAE
Ligand CL 3 x CL
Ligand NH4 1 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21
Unit cell:
a: 47.256Å b: 52.605Å c: 55.51Å
α: 90° β: 111.7° γ: 90°
R-values:
R R work R free
0.126 0.125 0.156
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

An Unexpected Species Determined by X-ray Crystallography that May Represent an Intermediate in the Reaction Catalyzed by Quinolinate Synthase.
Esakova et al. (2019)
1 more