› 4h9b

X-ray diffraction
1.2Å resolution

Radiation damage study of lysozyme - 0.70 MGy

Released:
DOI: 10.2210/pdb4h9b/pdb
PDB entry 4h9b coloured by chain, front view.
PDB entry 4h9b coloured by chain, side view.
PDB entry 4h9b coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Insights into the mechanism of X-ray-induced disulfide-bond cleavage in lysozyme crystals based on EPR, optical absorption and X-ray diffraction studies.
Sutton KA, Black PJ, Mercer KR, Garman EF, Owen RL, Snell EH, Bernhard WA
OpenAccess logo Acta Crystallogr D Biol Crystallogr 69 2381-94 (2013)
PMID: 24311579

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 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 3 x CL
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P43212
Unit cell:
a: 78.767Å b: 78.767Å c: 36.866Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.192 0.202

Quick links

Citations

2 review citations

From protein structure to function via single crystal optical spectroscopy.
Ronda et al. (2015)
1 more

2 mentions without citation

Insights into the mechanism of X-ray-induced disulfide-bond cleavage in lysozyme crystals based on EPR, optical absorption and X-ray diffraction studies.
Sutton et al. (2013)
1 more