7efs

X-ray diffraction
2.5Å resolution

Fructose-bisphosphate aldolase in Artemisia sieversiana pollen

Released:
Model geometry
Fit model/data
Source organism: Artemisia sieversiana
Entry authors: Li Z, Wei C, Ji Fu W, Zhi Qiang X

Function and Biology Details

Reaction catalysed:
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-104520 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 365 amino acids
Theoretical weight: 39.57 KDa
Source organism: Artemisia sieversiana
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: A0A2U1QAU9 (Residues: 1-357; Coverage: 100%)
Gene names: CTI12_AA053140, CTI12_AA368060
Sequence domains: Fructose-bisphosphate aldolase class-I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: BRUKER TURBO X-RAY SOURCE
Spacegroup: P212121
Unit cell:
a: 84.007Å b: 129.689Å c: 157.343Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.258
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'