› 1uc0

X-ray diffraction
1.85Å resolution

Crystal structure of wild-type hen-egg white lysozyme singly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine

Released:
DOI: 10.2210/pdb1uc0/pdb
PDB entry 1uc0 coloured by chain, front view.
PDB entry 1uc0 coloured by chain, side view.
PDB entry 1uc0 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
X-ray structural analysis of the ligand-recognition mechanism in the dual-affinity labeling of c-type lysozyme with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine.
Muraki M, Harata K
J Mol Recognit 16 72-82
PMID: 12720276

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
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: NAG, GAL
Carbohydrate polymer
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P43212
Unit cell:
a: 78.04Å b: 78.04Å c: 38.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.254

Quick links

Citations

3 citation in other articles

The CH/π hydrogen bond in chemistry. Conformation, supramolecules, optical resolution and interactions involving carbohydrates.
Nishio M. (2011)
2 more

2 mentions without citation

PEPOP: computational design of immunogenic peptides.
Moreau et al. (2008)
1 more