› 6rng

X-ray diffraction
2.15Å resolution

Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase

Released:
DOI: 10.2210/pdb6rng/pdb
PDB entry 6rng coloured by chain, front view.
PDB entry 6rng coloured by chain, side view.
PDB entry 6rng coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase
Wojciechowska I, Vogeli B, Shahar A, Szlachetko J, Gorka M, Sokolowska EM, Veyel D, Silva DV, Erb T, Zarivach R, Skirycz A
To be published

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase 6, cytosolic Chains: A, B, F, G
Molecule details ›
Chains: A, B, F, G
Length: 358 amino acids
Theoretical weight: 38.43 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia phage EcSzw-2
UniProt:
  • Canonical: Q9SJQ9 (Residues: 1-358; Coverage: 100%)
Gene names: At2g36460, FBA6
Sequence domains: Fructose-bisphosphate aldolase class-I

Ligands and Environments

3 bound ligands:
Ligand SO4 13 x SO4
Ligand GLY 3 x GLY
Ligand PRO 3 x PRO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 113.399Å b: 73.164Å c: 176.225Å
α: 90° β: 106.52° γ: 90°
R-values:
R R work R free
0.246 0.243 0.296
Expression system: Escherichia phage EcSzw-2

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