5i8l

X-ray diffraction
2.8Å resolution

Crystal structure of the full-length cell wall-binding module of Cpl7 mutant R223A

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 15.62 KDa
Source organism: Streptococcus phage CP-7
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P19385 (Residues: 199-342; Coverage: 42%)
Gene name: CPL7
Sequence domains: CW_7 repeat

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 29.524Å b: 50.331Å c: 86.089Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.289
Expression system: Escherichia coli BL21