› 1ov5

X-ray diffraction
2.1Å resolution

T4 Lysozyme Cavity Mutant L99a/M102Q Bound With 2-Allylphenol

Released:
DOI: 10.2210/pdb1ov5/pdb
PDB entry 1ov5 coloured by chain, front view.
PDB entry 1ov5 coloured by chain, side view.
PDB entry 1ov5 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Testing a flexible-receptor docking algorithm in a model binding site.
Wei BQ, Weaver LH, Ferrari AM, Matthews BW, Shoichet BK
J Mol Biol 337 1161-82 (2004)
PMID: 15046985

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: 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 CL 2 x CL
Ligand 2LP 1 x 2LP
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 60.8Å b: 60.8Å c: 96.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 not available not available
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Calculation of protein-ligand binding affinities.
Gilson et al. (2007)
17 more

1 mention without citation

Protein evolution along phylogenetic histories under structurally constrained substitution models.
Arenas et al. (2013)