› 1p37

X-ray diffraction
1.57Å resolution

T4 LYSOZYME CORE REPACKING BACK-REVERTANT L102M/CORE10

Released:
DOI: 10.2210/pdb1p37/pdb
PDB entry 1p37 coloured by chain, front view.
PDB entry 1p37 coloured by chain, side view.
PDB entry 1p37 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Repacking the Core of T4 lysozyme by automated design.
Mooers BH, Datta D, Baase WA, Zollars ES, Mayo SL, Matthews BW
J Mol Biol 332 741-56 (2003)
PMID: 12963380

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: 18.67 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 K 1 x K
Ligand CL 2 x CL
Ligand HED 1 x HED
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 59.49Å b: 59.49Å c: 96.208Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.221
Expression system: Escherichia coli

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Citations

5 review citations

Rational engineering of enzyme stability.
Eijsink et al. (2004)
4 more