4cu2

X-ray diffraction
2.11Å resolution

C-terminal domain of CTP1L endolysin mutant V195P that reduces autoproteolysis

Released:
Model geometry
Fit model/data

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
lysozyme Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 9 KDa
Source organism: Clostridium phage phiCTP1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D9ZNF3 (Residues: 195-274; Coverage: 29%)
Gene name: phiCTP1_gp29
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Spacegroup: I222
Unit cell:
a: 44.932Å b: 48.821Å c: 77.226Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.172 0.264
Expression system: Escherichia coli BL21(DE3)