› 1jse

X-ray diffraction
1.12Å resolution

FULL-MATRIX LEAST-SQUARES REFINEMENT OF TURKEY LYSOZYME

Released:
DOI: 10.2210/pdb1jse/pdb
PDB entry 1jse coloured by chain, front view.
PDB entry 1jse coloured by chain, side view.
PDB entry 1jse coloured by chain, top view.
Source organism: Meleagris gallopavo
Primary publication:
Full-matrix least-squares refinement of lysozymes and analysis of anisotropic thermal motion.
Harata K, Abe Y, Muraki M
Proteins 30 232-43 (1998)
PMID: 9517539

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.23 KDa
Source organism: Meleagris gallopavo
UniProt:
  • Canonical: P00703 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand POL 1 x POL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 38.15Å b: 33.32Å c: 46.24Å
α: 90° β: 110.14° γ: 90°
R-values:
R R work R free
0.104 not available 0.14

Quick links

Citations

2 review citations

Validation of protein models derived from experiment.
Laskowski et al. (1998)
1 more

1 mention without citation

Hypervalent nonbonded interactions of a divalent sulfur atom. Implications in protein architecture and the functions.
Iwaoka et al. (2012)