› 3fa0

X-ray diffraction
1.09Å resolution

Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant Arg96-->His

Released:
DOI: 10.2210/pdb3fa0/pdb
PDB entry 3fa0 coloured by chain, front view.
PDB entry 3fa0 coloured by chain, side view.
PDB entry 3fa0 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His.
Mooers BH, Tronrud DE, Matthews BW
Protein Sci 18 863-70 (2009)
PMID: 19384984

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: 162 amino acids
Theoretical weight: 18.44 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-162; Coverage: 99%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

5 bound ligands:
Ligand HED 1 x HED
Ligand BME 1 x BME
Ligand PO4 2 x PO4
Ligand CL 2 x CL
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P3221
Unit cell:
a: 60.37Å b: 60.37Å c: 96.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.148 0.188
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Interaction energy based protein structure networks.
Vijayabaskar et al. (2010)
3 more

9 mentions without citation

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