› 3oug

X-ray diffraction
1.55Å resolution

Crystal structure of cleaved L-aspartate-alpha-decarboxylase from Francisella tularensis

Released:
DOI: 10.2210/pdb3oug/pdb
PDB entry 3oug coloured by chain, front view.
PDB entry 3oug coloured by chain, side view.
PDB entry 3oug coloured by chain, top view.
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Entry authors: Nocek B, Gu M, Papazisi L, Anderson W, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
L-aspartate = beta-alanine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-177653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate 1-decarboxylase Chains: A, B, C, E, F, G, H, I
Molecule details ›
Chains: A, B, C, E, F, G, H, I
Length: 114 amino acids
Theoretical weight: 12.71 KDa
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5NF56 (Residues: 1-111; Coverage: 100%)
Gene names: FTT_1391, panD
Sequence domains: Aspartate decarboxylase
Structure domains: Barwin-like endoglucanases

Ligands and Environments

2 bound ligands:
Ligand CL 8 x CL
Ligand GOL 6 x GOL
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 79.934Å b: 80.525Å c: 85.025Å
α: 90° β: 104.33° γ: 90°
R-values:
R R work R free
0.18 0.172 0.197
Expression system: Escherichia coli

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