› 211l

X-ray diffraction
1.7Å resolution

PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME

Released:
DOI: 10.2210/pdb211l/pdb
PDB entry 211l coloured by chain, front view.
PDB entry 211l coloured by chain, side view.
PDB entry 211l coloured by chain, top view.
Source organism: Tequatrovirus T4
Primary publication:
Protein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme.
Vetter IR, Baase WA, Heinz DW, Xiong JP, Snow S, Matthews BW
Protein Sci 5 2399-415 (1996)
PMID: 8976549

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:
  • not assigned
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: 165 amino acids
Theoretical weight: 18.7 KDa
Source organism: Tequatrovirus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-108, 109-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand HED 1 x HED
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 60.97Å b: 60.97Å c: 97.14Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.173 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

3 mentions without citation

Genomic and proteomic analysis of invertebrate iridovirus type 9.
Wong et al. (2011)
2 more