› 1c6l

X-ray diffraction
1.9Å resolution

T4 LYSOZYME MUTANT C54T/C97A/L99A/F153A IN THE PRESENCE OF 8 ATM ARGON

Released:
DOI: 10.2210/pdb1c6l/pdb
PDB entry 1c6l coloured by chain, front view.
PDB entry 1c6l coloured by chain, side view.
PDB entry 1c6l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Size versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme.
Quillin ML, Breyer WA, Griswold IJ, Matthews BW
J Mol Biol 302 955-77 (2000)
PMID: 10993735

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: 18.51 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 3 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 61.123Å b: 61.123Å c: 97.161Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 not available not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

A review about nothing: are apolar cavities in proteins really empty?
Matthews et al. (2009)
5 more