› 1gyn

X-ray diffraction
2Å resolution

Class II fructose 1,6-bisphosphate aldolase with Cadmium (not Zinc) in the active site

Released:
DOI: 10.2210/pdb1gyn/pdb
PDB entry 1gyn coloured by chain, front view.
PDB entry 1gyn coloured by chain, side view.
PDB entry 1gyn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.
Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN
Acta Crystallogr D Biol Crystallogr 59 611-4 (2003)
PMID: 12595741

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142018 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase class 2 Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 39.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB71 (Residues: 2-359; Coverage: 100%)
Gene names: JW2892, b2925, fba, fbaA, fda
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand CD 5 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P6122
Unit cell:
a: 77.331Å b: 77.331Å c: 290.851Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.168 0.193
Expression system: Escherichia coli

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Citations

6 citation in other articles

Genome and low-iron response of an oceanic diatom adapted to chronic iron limitation.
Lommer et al. (2012)
5 more