› 3sb8

X-ray diffraction
2.65Å resolution

Cu-mediated Dimer of T4 Lysozyme D61H/K65H by Synthetic Symmetrization

Released:
DOI: 10.2210/pdb3sb8/pdb
PDB entry 3sb8 coloured by chain, front view.
PDB entry 3sb8 coloured by chain, side view.
PDB entry 3sb8 coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
An approach to crystallizing proteins by metal-mediated synthetic symmetrization.
Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO
Protein Sci 20 1876-90 (2011)
PMID: 21898649

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

Assemblies composition:
homo dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-133029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 165 amino acids
Theoretical weight: 18.64 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-162; Coverage: 99%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand CU 2 x CU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 44.88Å b: 95.18Å c: 117.02Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.222 0.273
Expression system: Escherichia coli

Quick links

Citations

9 review citations

The design of symmetric protein nanomaterials comes of age in theory and practice.
Yeates et al. (2016)
8 more