6fhg

X-ray diffraction
1.95Å resolution

Crystal structure of the Ts2631 endolysin from Thermus scotoductus phage with the unique N-terminal moiety responsible for peptidoglycan anchoring

Released:

Function and Biology Details

Reaction catalysed:
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-100688 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylmuramoyl-L-alanine amidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 156 amino acids
Theoretical weight: 18.1 KDa
Source organism: Thermus phage 2631
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A088FLK9 (Residues: 1-156; Coverage: 100%)
Sequence domains: N-acetylmuramoyl-L-alanine amidase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 53.579Å b: 56.094Å c: 116.715Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.247
Expression system: Escherichia coli