› 1lyh

X-ray diffraction
1.7Å resolution

DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59

Released:
DOI: 10.2210/pdb1lyh/pdb
PDB entry 1lyh coloured by chain, front view.
PDB entry 1lyh coloured by chain, side view.
PDB entry 1lyh coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59.
Bell JA, Becktel WJ, Sauer U, Baase WA, Matthews BW
Biochemistry 31 3590-6 (1992)
PMID: 1567817

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: 18.58 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: 61Å b: 61Å c: 96.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 not available not available
Expression system: Not provided

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Citations

5 review citations

Helix capping.
Aurora et al. (1998)
4 more