› 3c80

X-ray diffraction
1.99Å resolution

T4 Lysozyme mutant R96Y at room temperature

Released:
DOI: 10.2210/pdb3c80/pdb
PDB entry 3c80 coloured by chain, front view.
PDB entry 3c80 coloured by chain, side view.
PDB entry 3c80 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme.
Mooers BH, Baase WA, Wray JW, Matthews BW
Protein Sci 18 871-80 (2009)
PMID: 19384988

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 analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.67 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 BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 60.433Å b: 60.433Å c: 97.033Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 not available not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Lessons from the lysozyme of phage T4.
Baase et al. (2010)
1 more

4 mentions without citation

3D deep convolutional neural networks for amino acid environment similarity analysis.
Torng et al. (2017)
3 more