X-ray diffraction
2.4Å resolution

Structure of CutC choline lyase choline bound form from Klebsiella pneumoniae.


Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Choline trimethylamine-lyase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 795 amino acids
Theoretical weight: 89.48 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A0M3KL44 (Residues: 1-795; Coverage: 100%)
Gene name: cutC
Sequence domains:
Structure domains: Anaerobic Ribonucleotide-triphosphate Reductase Large Chain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P212121
Unit cell:
a: 89.41Å b: 221.87Å c: 419.48Å
α: 90° β: 90° γ: 90°
R R work R free
0.191 0.188 0.247
Expression system: Escherichia coli BL21(DE3)