3hde

X-ray diffraction
1.95Å resolution

Crystal structure of full-length endolysin R21 from phage 21

Released:
Source organism: Enterobacteria phage P21
Primary publication:
Regulation of a muralytic enzyme by dynamic membrane topology.
Nat Struct Mol Biol 16 1192-4 (2009)
PMID: 19881499

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SAR-endolysin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Enterobacteria phage P21
Expression system: Escherichia coli
UniProt:
  • Canonical: P27359 (Residues: 1-165; Coverage: 100%)
Gene name: R
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 78.249Å b: 94.814Å c: 97.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.248
Expression system: Escherichia coli