› 1dyb

X-ray diffraction
1.75Å resolution

DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME

Released:
DOI: 10.2210/pdb1dyb/pdb
PDB entry 1dyb coloured by chain, front view.
PDB entry 1dyb coloured by chain, side view.
PDB entry 1dyb coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
Blaber M, Zhang XJ, Lindstrom JD, Pepiot SD, Baase WA, Matthews BW
J Mol Biol 235 600-24 (1994)
PMID: 8289284

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: 18.62 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
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 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 61.3Å b: 61.3Å c: 96.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 not available not available
Expression system: Not provided

Quick links

Citations

7 review citations

Principles of protein folding--a perspective from simple exact models.
Dill et al. (1995)
6 more