› 3q94

X-ray diffraction
2.3Å resolution

The crystal structure of fructose 1,6-bisphosphate aldolase from Bacillus anthracis str. 'Ames Ancestor'

Released:
DOI: 10.2210/pdb3q94/pdb
PDB entry 3q94 coloured by chain, front view.
PDB entry 3q94 coloured by chain, side view.
PDB entry 3q94 coloured by chain, top view.
Source organism: Bacillus anthracis str. 'Ames Ancestor'
Entry authors: Tan K, Zhou M, Kwon K, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-105628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase, class II Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 31.4 KDa
Source organism: Bacillus anthracis str. 'Ames Ancestor'
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A6H3AA11 (Residues: 1-285; Coverage: 100%)
Gene names: GBAA_5580, fba2
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand ZN 10 x ZN
Ligand NA 2 x NA
Ligand 13P 2 x 13P
Ligand ACT 4 x ACT
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3121
Unit cell:
a: 95.155Å b: 95.155Å c: 155.967Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.166 0.222
Expression system: Escherichia coli

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