› 4ekq

X-ray diffraction
1.54Å resolution

T4 Lysozyme L99A/M102H with 4-Nitrophenol Bound

Released:
DOI: 10.2210/pdb4ekq/pdb
PDB entry 4ekq coloured by chain, front view.
PDB entry 4ekq coloured by chain, side view.
PDB entry 4ekq coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
Engineering a model protein cavity to catalyze the Kemp elimination.
Merski M, Shoichet BK
Proc Natl Acad Sci U S A 109 16179-83 (2012)
PMID: 22988064

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: 187 amino acids
Theoretical weight: 21.4 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

5 bound ligands:
Ligand BME 2 x BME
Ligand NPO 3 x NPO
Ligand SO4 5 x SO4
Ligand HED 1 x HED
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 48.21Å b: 76.07Å c: 52.81Å
α: 90° β: 93.01° γ: 90°
R-values:
R R work R free
0.176 0.175 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

De novo enzymes by computational design.
Kries et al. (2013)
8 more

2 mentions without citation

Engineering a model protein cavity to catalyze the Kemp elimination.
Merski et al. (2012)
1 more