1bvk

X-ray diffraction
2.7Å resolution

HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH LYSOZYME

Released:

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-224919 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HULYS11 Chains: A, D
Molecule details ›
Chains: A, D
Length: 108 amino acids
Theoretical weight: 11.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
HULYS11 Chains: B, E
Molecule details ›
Chains: B, E
Length: 117 amino acids
Theoretical weight: 12.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Lysozyme C Chains: C, F
Molecule details ›
Chains: C, F
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • 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: RIGAKU RUH2R
Spacegroup: P41212
Unit cell:
a: 97.7Å b: 97.7Å c: 174.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.297
Expression system: Escherichia coli