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X-ray diffraction
1.7Å resolution

Crystal structure of 6-phosphogluconolactonase from Leishmania guyanensis

Released:
Primary publication:
Optimal description of a protein structure in terms of multiple groups undergoing TLS motion.
Acta Crystallogr D Biol Crystallogr 62 439-50 (2006)
PMID: 16552146

Function and Biology Details

Reaction catalysed:
6-phospho-D-glucono-1,5-lactone + H(2)O = 6-phospho-D-gluconate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-107313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphogluconolactonase Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 28.69 KDa
Source organism: Leishmania braziliensis MHOM/BR/75/M2904
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A4HFB4 (Residues: 1-267; Coverage: 100%)
Gene names: LBRM_26_2630, LBRM_26_2660
Sequence domains: Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 69.999Å b: 89.381Å c: 100.521Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.185
Expression system: Escherichia coli BL21(DE3)