1qsa

X-ray diffraction
1.65Å resolution

CRYSTAL STRUCTURE OF THE 70 KDA SOLUBLE LYTIC TRANSGLYCOSYLASE SLT70 FROM ESCHERICHIA COLI AT 1.65 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-142803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble lytic murein transglycosylase Chain: A
Molecule details ›
Chain: A
Length: 618 amino acids
Theoretical weight: 70.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGC3 (Residues: 28-645; Coverage: 100%)
Gene names: JW4355, b4392, slt, sltY
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 78.009Å b: 87.477Å c: 132.906Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.191
Expression system: Escherichia coli