› 3gum

X-ray diffraction
2.24Å resolution

T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--p-xylene binding

Released:
DOI: 10.2210/pdb3gum/pdb
PDB entry 3gum coloured by chain, front view.
PDB entry 3gum coloured by chain, side view.
PDB entry 3gum coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Use of stabilizing mutations to engineer a charged group within a ligand-binding hydrophobic cavity in T4 lysozyme.
Liu L, Baase WA, Michael MM, Matthews BW
Biochemistry 48 8842-51 (2009)
PMID: 19663503

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.71 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

4 bound ligands:
Ligand PXY 2 x PXY
Ligand CL 3 x CL
Ligand ACT 2 x ACT
Ligand CA 1 x CA
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P43
Unit cell:
a: 49.709Å b: 49.709Å c: 129.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.264
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Lessons from the lysozyme of phage T4.
Baase et al. (2010)
1 more

1 mention without citation

Identifying ligand binding sites and poses using GPU-accelerated Hamiltonian replica exchange molecular dynamics.
Wang et al. (2013)