› 3cdq

X-ray diffraction
1.68Å resolution

Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme

Released:
DOI: 10.2210/pdb3cdq/pdb
PDB entry 3cdq coloured by chain, front view.
PDB entry 3cdq coloured by chain, side view.
PDB entry 3cdq 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 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

3 bound ligands:
Ligand CL 2 x CL
Ligand K 1 x K
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 60.927Å b: 60.927Å c: 97.389Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

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