4pk0

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF T4 LYSOZYME-PEPTIDE IN COMPLEX WITH TEICOPLANIN-A2-2

Released:

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
TEICOPLANIN-A2-2 Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 1.21 KDa
Source organism: Actinoplanes teichomyceticus
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.34 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: D9IEF7 (Residues: 1-164; Coverage: 100%)
Gene names: T4Tp126, e
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I222
Unit cell:
a: 55.923Å b: 63.233Å c: 138.615Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.237
Expression system: Escherichia coli