› 7l3c

X-ray diffraction
1.31Å resolution

T4 Lysozyme L99A - o-xylene - RT

Released:
DOI: 10.2210/pdb7l3c/pdb
PDB entry 7l3c coloured by chain, front view.
PDB entry 7l3c coloured by chain, side view.
PDB entry 7l3c coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Temperature artifacts in protein structures bias ligand-binding predictions.
Bradford SYC, El Khoury L, Ge Y, Osato M, Mobley DL, Fischer M
Chem Sci 12 11275-11293 (2021)
PMID: 34667539

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: 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

Ligands and Environments

4 bound ligands:
Ligand TRS 1 x TRS
Ligand CL 1 x CL
Ligand BME 1 x BME
Ligand OXE 1 x OXE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 61.038Å b: 61.038Å c: 97.896Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.153 0.152 0.177
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Prioritizing Small Sets of Molecules for Synthesis through in-silico Tools: A Comparison of Common Ranking Methods.
Breznik et al. (2023)
12 more

1 mention without citation

Temperature artifacts in protein structures bias ligand-binding predictions.
Bradford et al. (2021)