› 1qth

X-ray diffraction
1.9Å resolution

THE INTRODUCTION OF STRAIN AND ITS EFFECTS ON THE STRUCTURE AND STABILITY OF T4 LYSOZYME

Released:
DOI: 10.2210/pdb1qth/pdb
PDB entry 1qth coloured by chain, front view.
PDB entry 1qth coloured by chain, side view.
PDB entry 1qth coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
The introduction of strain and its effects on the structure and stability of T4 lysozyme.
Liu R, Baase WA, Matthews BW
J Mol Biol 295 127-45 (2000)
PMID: 10623513

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.69 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
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
X-ray source: RIGAKU
Spacegroup: P31
Unit cell:
a: 53.569Å b: 53.569Å c: 101.871Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli

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Citations

1 review citation

Frustration in biomolecules.
Ferreiro et al. (2014)
35 other articles