› 3mmt

X-ray diffraction
2.35Å resolution

Crystal structure of fructose bisphosphate aldolase from Bartonella henselae, bound to fructose bisphosphate

Released:
DOI: 10.2210/pdb3mmt/pdb
PDB entry 3mmt coloured by chain, front view.
PDB entry 3mmt coloured by chain, side view.
PDB entry 3mmt coloured by chain, top view.
Source organism: Bartonella henselae
Primary publication:
Structure of fructose bisphosphate aldolase from Bartonella henselae bound to fructose 1,6-bisphosphate.
Gardberg A, Abendroth J, Bhandari J, Sankaran B, Staker B
OpenAccess logo Acta Crystallogr Sect F Struct Biol Cryst Commun 67 1051-4 (2011)
PMID: 21904049

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185242 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 347 amino acids
Theoretical weight: 37.56 KDa
Source organism: Bartonella henselae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8L207 (Residues: 1-343; Coverage: 100%)
Gene name: fbab
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 2FP 4 x 2FP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 72.39Å b: 127.71Å c: 157.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.222
Expression system: Escherichia coli BL21(DE3)

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Citations

4 mentions without citation

Interaction network and mass spectrometry data of Xanthomonas citri subsp. citri surface proteins from differential proteomic analysis of infectious and non-infectious cells.
Carnielli et al. (2016)
3 more