› 1aj8

X-ray diffraction
1.9Å resolution

CITRATE SYNTHASE FROM PYROCOCCUS FURIOSUS

Released:
DOI: 10.2210/pdb1aj8/pdb
PDB entry 1aj8 coloured by chain, front view.
PDB entry 1aj8 coloured by chain, side view.
PDB entry 1aj8 coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
The crystal structure of citrate synthase from the hyperthermophilic archaeon pyrococcus furiosus at 1.9 A resolution,
Russell RJ, Ferguson JM, Hough DW, Danson MJ, Taylor GL
Biochemistry 36 9983-94 (1997)
PMID: 9254593

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Citrate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 371 amino acids
Theoretical weight: 42.34 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q53554 (Residues: 7-377; Coverage: 98%)
Gene names: PF0203, gltA
Sequence domains: Citrate synthase, C-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand COA 2 x COA
Ligand CIT 2 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P41212
Unit cell:
a: 98.29Å b: 98.29Å c: 238.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.232
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
18 more

3 mentions without citation

Arpeggio: A Web Server for Calculating and Visualising Interatomic Interactions in Protein Structures.
Jubb et al. (2017)
2 more