3hjz

X-ray diffraction
1.9Å resolution

The structure of an aldolase from Prochlorococcus marinus

Released:

Function and Biology Details

Reaction catalysed:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174260 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 37.68 KDa
Source organism: Prochlorococcus marinus str. MIT 9312
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q31C15 (Residues: 1-333; Coverage: 100%)
Gene names: PMT9312_0519, tal
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 42.755Å b: 80.376Å c: 97.866Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.156 0.203
Expression system: Escherichia coli BL21(DE3)