› 193l

X-ray diffraction
1.33Å resolution

THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME

Released:
DOI: 10.2210/pdb193l/pdb
PDB entry 193l coloured by chain, front view.
PDB entry 193l coloured by chain, side view.
PDB entry 193l coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission.
Vaney MC, Maignan S, Riès-Kautt M, Ducriux A
Acta Crystallogr D Biol Crystallogr 52 505-17 (1996)
PMID: 15299672

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-132831 (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:
Ligand CL 1 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P43212
Unit cell:
a: 78.54Å b: 78.54Å c: 37.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.226

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Citations

5 review citations

Expanding coordination chemistry from protein to protein assembly.
Sanghamitra et al. (2013)
4 more

71 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
70 more