› 2f30

X-ray diffraction
1.65Å resolution

Triclinic cross-linked Lysozyme soaked with 4.5M urea

Released:
DOI: 10.2210/pdb2f30/pdb
PDB entry 2f30 coloured by chain, front view.
PDB entry 2f30 coloured by chain, side view.
PDB entry 2f30 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
On the edge of the denaturation process: application of X-ray diffraction to barnase and lysozyme cross-linked crystals with denaturants in molar concentrations.
Salem M, Mauguen Y, Prangé T
Biochim Biophys Acta 1764 903-12 (2006)
PMID: 16600702

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 NO3 6 x NO3
Ligand URE 2 x URE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P1
Unit cell:
a: 27.11Å b: 31.94Å c: 34.17Å
α: 88.15° β: 108.62° γ: 111.73°
R-values:
R R work R free
0.169 0.15 0.191

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Citations

6 citation in other articles

Counteraction of urea by trimethylamine N-oxide is due to direct interaction.
Meersman et al. (2009)
5 more