› 152l

X-ray diffraction
2Å resolution

CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME

Released:
DOI: 10.2210/pdb152l/pdb
PDB entry 152l coloured by chain, front view.
PDB entry 152l coloured by chain, side view.
PDB entry 152l coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme.
Zhang XJ, Matthews BW
Protein Sci 3 1031-9 (1994)
PMID: 7920248

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: 18.63 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-163; Coverage: 99%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 63.2Å b: 51Å c: 48.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 not available not available
Expression system: Not provided

Quick links

Citations

6 review citations

Locating and characterizing binding sites on proteins.
Mattos et al. (1996)
5 more

5 mentions without citation

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