› 4zpu

X-ray diffraction
2.4Å resolution

The structure of DLP12 endolysin exhibits likely active and inactive conformations.

Released:
DOI: 10.2210/pdb4zpu/pdb
PDB entry 4zpu coloured by chain, front view.
PDB entry 4zpu coloured by chain, side view.
PDB entry 4zpu coloured by chain, top view.
Source organism: Escherichia coli K-12
Entry authors: Kesavan B, Arockiasamy A, Krishnaswamy S

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160220 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme RrrD Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 175 amino acids
Theoretical weight: 19.05 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P78285 (Residues: 1-165; Coverage: 100%)
Gene names: JW0544, arrD, b0555, rrrD, ybcS
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
Ligand ACT 4 x ACT
Ligand FMT 2 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 78.106Å b: 94.131Å c: 97.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.285
Expression system: Escherichia coli

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