3clm

X-ray diffraction
1.14Å resolution

Crystal structure of transaldolase (YP_208650.1) from Neisseria gonorrhoeae FA 1090 at 1.14 A resolution

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177060 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chain: A
Molecule details ›
Chain: A
Length: 352 amino acids
Theoretical weight: 37.79 KDa
Source organism: Neisseria gonorrhoeae FA 1090
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5F6E9 (Residues: 1-351; Coverage: 100%)
Gene names: NGO1610, tal
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1, APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 42.14Å b: 83.03Å c: 89.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.131 0.13 0.161
Expression system: Escherichia coli