› 1ivm

Solution NMR

Solution structure of mouse lysozyme M

Released:
DOI: 10.2210/pdb1ivm/pdb
PDB entry 1ivm coloured by chain, ensemble of 20 models, front view.
PDB entry 1ivm coloured by chain, ensemble of 20 models, side view.
PDB entry 1ivm coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Solution structure and activity of mouse lysozyme M.
Obita T, Ueda T, Imoto T
Cell Mol Life Sci 60 176-84 (2003)
PMID: 12613666

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-140421 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C-2 Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 14.84 KDa
Source organism: Mus musculus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P08905 (Residues: 19-148; Coverage: 100%)
Gene names: Lyz, Lyz2, Lyzs
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing
Expression system: Komagataella pastoris

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Citations

2 review citations

Lysozymes in the animal kingdom.
Callewaert et al. (2010)
1 more

1 mention without citation

Towards comprehensive analysis of protein family quantitative stability-flexibility relationships using homology models.
Verma et al. (2014)