› 4rxg

X-ray diffraction
2.15Å resolution

Fructose-6-phosphate aldolase Q59E from E.coli

Released:
DOI: 10.2210/pdb4rxg/pdb
PDB entry 4rxg coloured by chain, front view.
PDB entry 4rxg coloured by chain, side view.
PDB entry 4rxg coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Acid Base Catalyst Discriminates between a Fructose 6-Phosphate Aldolase and a Transaldolase
Stellmacher L, Sandalova T, Leptihn S, Schneider G, Sprenger GA, Samland AK
ChemCatChem (2015)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-6-phosphate aldolase 1 Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 220 amino acids
Theoretical weight: 23.02 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P78055 (Residues: 1-220; Coverage: 100%)
Gene names: JW5109, b0825, fsa, fsaA, mipB, ybiZ
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand GOL 20 x GOL
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P212121
Unit cell:
a: 115.436Å b: 126.748Å c: 183.448Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.228
Expression system: Escherichia coli DH5[alpha]

Quick links