X-ray diffraction
2.2Å resolution

Crystal structure of putative fructose-1,6-bisphosphate aldolase from Candida auris

Source organism: [Candida] auris
Entry authors: Stogios PJ, Evdokimova E, Tan K, Di Leo R, Joachimiak A, Satchell KJF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Fructose-bisphosphate aldolase Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 39.41 KDa
Source organism: [Candida] auris
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A5C1DZF7 (Residues: 1-357; Coverage: 100%)
Gene names: CAJCM15448_14580, CJI96_0004025, QG37_01471
Sequence domains: Fructose-bisphosphate aldolase class-II

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6522
Unit cell:
a: 64.477Å b: 64.477Å c: 320.77Å
α: 90° β: 90° γ: 120°
R R work R free
0.198 0.194 0.238
Expression system: Escherichia coli BL21(DE3)