› 3byq

X-ray diffraction
1.7Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102100 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amino acid synthesis family protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 193 amino acids
Theoretical weight: 21.41 KDa
Source organism: Bordetella bronchiseptica RB50
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3LTD0 (Residues: 1-192; Coverage: 100%)
Gene name: BB2672
Sequence domains: Amino acid synthesis
Structure domains: BB2672

Ligands and Environments

3 bound ligands:
Ligand CL 4 x CL
Ligand PG4 2 x PG4
Ligand EDO 27 x EDO
1 modified residue:
Ligand MSE 27 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2221
Unit cell:
a: 96.542Å b: 133.127Å c: 92.544Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.138 0.169
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Elucidation of the trigonelline degradation pathway reveals previously undescribed enzymes and metabolites.
Perchat et al. (2018)
1 more

1 mention without citation

Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism.
Bakolitsa et al. (2010)