4i0c

X-ray diffraction
1.95Å resolution

The structure of the camelid antibody cAbHuL5 in complex with human 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
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-211422 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysozyme C Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.72 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P61626 (Residues: 19-148; Coverage: 100%)
Gene names: LYZ, LZM
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
cAbHuL5 antibody Chains: C, D
Molecule details ›
Chains: C, D
Length: 132 amino acids
Theoretical weight: 14.6 KDa
Source organism: Camelus dromedarius
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P43212
Unit cell:
a: 96.321Å b: 96.321Å c: 156.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.219
Expression systems:
  • Komagataella pastoris
  • Escherichia coli