4wly

X-ray diffraction
1.62Å resolution

High pressure protein crystallography of hen egg white lysozyme at 380 MPa

Released:
Source organism: Gallus gallus
Primary publication:
High-pressure protein crystallography of hen egg-white lysozyme.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 71 742-53 (2015)
PMID: 25849385

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P43212
Unit cell:
a: 77.51Å b: 77.51Å c: 37.967Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.155 0.194