PDBe 2eql

X-ray diffraction
2.5Å resolution

CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C, milk isozyme Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.67 KDa
Source organism: Equus caballus
Expression system: Not provided
UniProt:
  • Canonical: P11376 (Residues: 1-129; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 54.1Å b: 57.2Å c: 38.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 not available
Expression system: Not provided