› 247l

X-ray diffraction
1.75Å resolution

THE RESPONSE OF T4 LYSOZYME TO LARGE-TO-SMALL SUBSTITUTIONS WITHIN THE CORE AND ITS RELATION TO THE HYDROPHOBIC EFFECT

Released:
DOI: 10.2210/pdb247l/pdb
PDB entry 247l coloured by chain, front view.
PDB entry 247l coloured by chain, side view.
PDB entry 247l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.
Xu J, Baase WA, Baldwin E, Matthews BW
Protein Sci 7 158-77 (1998)
PMID: 9514271

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: 18.59 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

2 bound ligands:
Ligand CL 2 x CL
Ligand HED 1 x HED
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 60.91Å b: 60.91Å c: 97.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.16 not available
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Structural symmetry and protein function.
Goodsell et al. (2000)
15 more

2 mentions without citation

Variation in the prion protein gene (PRNP) sequence of wild deer in Great Britain and mainland Europe.
Robinson et al. (2019)
1 more