2wwc

X-ray diffraction
1.75Å resolution

3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,4-beta-N-acetylmuramidase Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 55.27 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8DP07 (Residues: 34-501; Coverage: 100%)
Gene names: lytC, spr1431
Sequence domains: Glycosyl hydrolases family 25
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 59.54Å b: 68.8Å c: 75.64Å
α: 90° β: 105.45° γ: 90°
R-values:
R R work R free
0.176 0.174 0.203
Expression system: Escherichia coli BL21