› 5ktt

X-ray diffraction
1.5Å resolution

Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound L-malate and Fe4S4 cluster

Released:
DOI: 10.2210/pdb5ktt/pdb
PDB entry 5ktt coloured by chain, front view.
PDB entry 5ktt coloured by chain, side view.
PDB entry 5ktt 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

2 bound ligands:
Ligand SF4 1 x SF4
Ligand LMR 1 x LMR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 47.333Å b: 54.639Å c: 55.613Å
α: 90° β: 90.79° γ: 90°
R-values:
R R work R free
0.148 0.146 0.193
Expression system: Escherichia coli BL21(DE3)

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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