PDBe 2nwd

X-ray diffraction
1.04Å resolution

Structure of chemically synthesized human lysozyme at 1 Angstrom resolution

Released:
Source organism: Homo sapiens
Primary publication:
Convergent chemical synthesis and high-resolution x-ray structure of human lysozyme.
Proc. Natl. Acad. Sci. U.S.A. 104 4846-51 (2007)
PMID: 17360367

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: X
Molecule details ›
Chain: X
Length: 130 amino acids
Theoretical weight: 14.72 KDa
Source organism: Homo sapiens
Expression system: Not provided
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: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 56.261Å b: 61.133Å c: 32.851Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.133 0.152
Expression system: Not provided