PDBe 3ln2

X-ray diffraction
2.04Å resolution

Crystal Structure of a Charge Engineered Human Lysozyme Variant

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
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.66 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61626 (Residues: 19-148; Coverage: 100%)
Gene names: LYZ, LZM
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
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 42.421Å b: 63.795Å c: 111.077Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.222
Expression system: Saccharomyces cerevisiae