PDBe 1am7

X-ray diffraction
2.3Å resolution

Lysozyme from bacteriophage lambda

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 158 amino acids
Theoretical weight: 17.86 KDa
Source organism: Escherichia virus Lambda
Expression system: Escherichia coli
UniProt:
  • Canonical: P03706 (Residues: 1-158; Coverage: 100%)
Gene name: R
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 73.01Å b: 78.8Å c: 82.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.163 0.213
Expression system: Escherichia coli