› 1l89

X-ray diffraction
1.9Å resolution

SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES

Released:
DOI: 10.2210/pdb1l89/pdb
PDB entry 1l89 coloured by chain, front view.
PDB entry 1l89 coloured by chain, side view.
PDB entry 1l89 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences.
Eriksson AE, Baase WA, Matthews BW
J Mol Biol 229 747-69 (1993)
PMID: 8433369

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: 18.51 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: 61.4Å b: 61.4Å c: 95.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 not available not available
Expression system: Not provided

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Citations

7 review citations

An analysis of packing in the protein folding problem.
Richards et al. (1993)
6 more