X-ray diffraction
1.8Å resolution

Crystal structure of Brucella abortus PliC in complex with human lysozyme

Source organism: Homo sapiens

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysozyme C Chains: A, C
Molecule details ›
Chains: A, C
Length: 130 amino acids
Theoretical weight: 14.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P61626 (Residues: 19-148; Coverage: 100%)
Gene names: LYZ, LZM
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
Humanlysozyme Chains: B, D
Molecule details ›
Chains: B, D
Length: 99 amino acids
Theoretical weight: 10.65 KDa
Source organism: Homo sapiens
Expression system: Oryza sativa
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P21212
Unit cell:
a: 100.253Å b: 88.984Å c: 66.206Å
α: 90° β: 90° γ: 90°
R R work R free
0.187 0.186 0.222
Expression systems:
  • Escherichia coli
  • Oryza sativa