› 3cdo

X-ray diffraction
1.87Å resolution

Bacteriophage T4 lysozyme mutant R96V in wildtype background at low temperature

Released:
DOI: 10.2210/pdb3cdo/pdb
PDB entry 3cdo coloured by chain, front view.
PDB entry 3cdo coloured by chain, side view.
PDB entry 3cdo 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)
Assembly name:
PDBe Complex ID:
PDB-CPX-133020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 164 amino acids
Theoretical weight: 18.6 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

3 bound ligands:
Ligand HEZ 4 x HEZ
Ligand MPD 4 x MPD
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 57.82Å b: 99.316Å c: 123.012Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.231
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Protein dynamic communities from elastic network models align closely to the communities defined by molecular dynamics.
Mishra et al. (2018)
1 more