› 1l39

X-ray diffraction
1.85Å resolution

CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS

Released:
DOI: 10.2210/pdb1l39/pdb
PDB entry 1l39 coloured by chain, front view.
PDB entry 1l39 coloured by chain, side view.
PDB entry 1l39 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Sun DP, Sauer U, Nicholson H, Matthews BW
Biochemistry 30 7142-53 (1991)
PMID: 1854726

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-133020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.64 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 61.1Å b: 61.1Å c: 96.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 not available not available
Expression system: Not provided

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Citations

12 review citations

The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.
Serrano et al. (1992)
11 more