› 2dqa

X-ray diffraction
1.6Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184841 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Invertebrate-type lysozyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 13.88 KDa
Source organism: Ruditapes philippinarum
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q8IU26 (Residues: 12-134; Coverage: 98%)
Sequence domains: Destabilase
Structure domains: Lysozyme

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand PT 8 x PT
Ligand BGC 2 x BGC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1, BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 42.749Å b: 88.76Å c: 43.644Å
α: 90° β: 116.04° γ: 90°
R-values:
R R work R free
0.176 0.175 0.21
Expression system: Komagataella pastoris

Quick links

Citations

3 review citations

Lysozymes in the animal kingdom.
Callewaert et al. (2010)
2 more

6 mentions without citation

Decoding an Amino Acid Sequence to Extract Information on Protein Folding.
Kikuchi T. (2022)
5 more