› 1ps5

X-ray diffraction
2Å resolution

STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1ps5/pdb
PDB entry 1ps5 coloured by chain, front view.
PDB entry 1ps5 coloured by chain, side view.
PDB entry 1ps5 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Enhancing protein crystallization through precipitant synergy.
Majeed S, Ofek G, Belachew A, Huang CC, Zhou T, Kwong PD
Structure 11 1061-70 (2003)
PMID: 12962625

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

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 42.944Å b: 53.143Å c: 50.211Å
α: 90° β: 97.32° γ: 90°
R-values:
R R work R free
0.189 0.189 0.25

Quick links

Citations

3 review citations

An overview of biological macromolecule crystallization.
Russo Krauss et al. (2013)
2 more

2 mentions without citation

Hen egg-white lysozyme crystallisation: protein stacking and structure stability enhanced by a Tellurium(VI)-centred polyoxotungstate.
Bijelic et al. (2015)
1 more