PDBe 2zwb

Neutron Diffraction
1.8Å resolution

Neutron crystal structure of wild type human lysozyme in D2O

Released:
Source organism: Homo sapiens
Entry authors: Chiba-Kamoshida K, Matsui T, Chatake T, Ohhara T, Ostermann A, Tanaka I, Yutani K, Niimura N

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: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 14.72 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Spacegroup: P212121
Unit cell:
a: 33.825Å b: 56.883Å c: 60.965Å α: 90° β: 90° γ: 90°
R-values:
R R work R free 0.223 0.223 0.247
Expression system: Komagataella pastoris