› 1l6w

X-ray diffraction
1.93Å resolution

Function and Biology Details

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

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
Expression system: Escherichia coli
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

1 bound ligand:
Ligand GOL 10 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 115.49Å b: 126.94Å c: 183.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.213
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Microbial aldolases as C-C bonding enzymes--unknown treasures and new developments.
Samland et al. (2006)
5 more

6 mentions without citation

Dead-end elimination with perturbations (DEEPer): a provable protein design algorithm with continuous sidechain and backbone flexibility.
Hallen et al. (2013)
5 more