› 7loe

X-ray diffraction
1.01Å resolution

T4 lysozyme mutant L99A in complex with 1-fluoranylnaphthalene

Released:
DOI: 10.2210/pdb7loe/pdb
PDB entry 7loe coloured by chain, front view.
PDB entry 7loe coloured by chain, side view.
PDB entry 7loe coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Energy penalties enhance flexible receptor docking in a model cavity.
Kamenik AS, Singh I, Lak P, Balius TE, Liedl KR, Shoichet BK
Proc Natl Acad Sci U S A 118 (2021)
PMID: 34475217

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 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: 172 amino acids
Theoretical weight: 19.69 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme

Ligands and Environments

3 bound ligands:
Ligand Y84 1 x Y84
Ligand BME 1 x BME
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3221
Unit cell:
a: 60.078Å b: 60.078Å c: 96.266Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.204 0.219
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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Citations

2 review citations

Fragment-based drug discovery-the importance of high-quality molecule libraries.
Bon et al. (2022)
1 more

1 mention without citation

Energy penalties enhance flexible receptor docking in a model cavity.
Kamenik et al. (2021)