› 254l

X-ray diffraction
1.9Å resolution

LYSOZYME

Released:
DOI: 10.2210/pdb254l/pdb
PDB entry 254l coloured by chain, front view.
PDB entry 254l coloured by chain, side view.
PDB entry 254l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
A relationship between protein stability and protein function.
Shoichet BK, Baase WA, Kuroki R, Matthews BW
Proc Natl Acad Sci U S A 92 452-6 (1995)
PMID: 7831309

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: 18.6 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

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 RUH2R
Spacegroup: P3221
Unit cell:
a: 61Å b: 61Å c: 97.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.158 not available
Expression system: Escherichia coli

Quick links

Citations

56 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
55 more

1 mention without citation

Transcriptome Analysis of the Spodoptera frugiperda Ascovirus In Vivo Provides Insights into How Its Apoptosis Inhibitors and Caspase Promote Increased Synthesis of Viral Vesicles and Virion Progeny.
Zaghloul et al. (2017)