PDBe 1d3f

X-ray diffraction
2.05Å resolution

N-TERMINAL DOMAIN CORE METHIONINE MUTATION

Released:
Source organism: Escherichia virus T4
Primary publication:
Use of differentially substituted selenomethionine proteins in X-ray structure determination.
Acta Crystallogr. D Biol. Crystallogr. 55 1967-70 (1999)
PMID: 10666571

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:

Structure analysis Details

Assembly composition:
monomeric (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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 60.97Å b: 60.97Å c: 97.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.159 not available
Expression system: Escherichia coli