› 3hua

X-ray diffraction
1.4Å resolution

4,5,6,7-tetrahydroindole in complex with T4 lysozyme L99A/M102Q

Released:
DOI: 10.2210/pdb3hua/pdb
PDB entry 3hua coloured by chain, front view.
PDB entry 3hua coloured by chain, side view.
PDB entry 3hua coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Predicting ligand binding affinity with alchemical free energy methods in a polar model binding site.
Boyce SE, Mobley DL, Rocklin GJ, Graves AP, Dill KA, Shoichet BK
J Mol Biol 394 747-63 (2009)
PMID: 19782087

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: 18.65 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 JZ9 1 x JZ9
Ligand BME 2 x BME
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3221
Unit cell:
a: 60.327Å b: 60.327Å c: 97.438Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.173 0.192
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Entropy-enthalpy compensation: role and ramifications in biomolecular ligand recognition and design.
Chodera et al. (2013)
9 more

2 mentions without citation

Predicting Binding Free Energies: Frontiers and Benchmarks.
Mobley et al. (2017)
1 more