› 5a3z

X-ray diffraction
1.59Å resolution

Structure of monoclinic Lysozyme obtained by multi crystal data collection

Released:
DOI: 10.2210/pdb5a3z/pdb
Model geometry
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PDB entry 5a3z coloured by chain, front view.
PDB entry 5a3z coloured by chain, side view.
PDB entry 5a3z coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines.
Zander U, Bourenkov G, Popov AN, de Sanctis D, Svensson O, McCarthy AA, Round E, Gordeliy V, Mueller-Dieckmann C, Leonard GA
OpenAccess logo Acta Crystallogr D Biol Crystallogr 71 2328-43 (2015)
PMID: 26527148

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:
  • not assigned
Cellular component:
  • not assigned
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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 147 amino acids
Theoretical weight: 16.26 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 1-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand NO3 2 x NO3
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 27.583Å b: 62.638Å c: 59.553Å
α: 90° β: 91.06° γ: 90°
R-values:
R R work R free
0.216 0.213 0.265

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Citations

3 review citations

Best practices for time-resolved serial synchrotron crystallography.
Schulz et al. (2022)
2 more

1 mention without citation

MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines.
Zander et al. (2015)

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