X-ray diffraction
1.6Å resolution

Structure of ivy complexed with its target, HEWL


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 tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Inhibitor of vertebrate lysozyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 14.97 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P0AD59 (Residues: 29-157; Coverage: 100%)
Gene names: JW0210, b0220, ivy, ykfE
Sequence domains: Inhibitor of vertebrate lysozyme (Ivy)
Structure domains: Inhibitor of vertebrate lysozyme
Lysozyme C Chains: C, D
Molecule details ›
Chains: C, D
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 55.49Å b: 59.56Å c: 69.2Å
α: 90° β: 95.39° γ: 90°
R R work R free
0.181 0.181 0.212
Expression system: Escherichia coli