1qdt

X-ray diffraction
2.1Å resolution

2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOYSLASE SLT35 IN COMPLEX WITH CALCIUM

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-154236 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-bound lytic murein transglycosylase B Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 36.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P41052 (Residues: 40-361; Coverage: 94%)
Gene names: JW2671, b2701, mltB
Sequence domains: Transglycosylase SLT domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 58.417Å b: 67.788Å c: 99.149Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.206
Expression system: Escherichia coli