1vfb

X-ray diffraction
1.8Å resolution

BOUND WATER MOLECULES AND CONFORMATIONAL STABILIZATION HELP MEDIATE AN ANTIGEN-ANTIBODY ASSOCIATION

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-132833 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Immunoglobulin kappa chain variable 12-41 Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.7 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01635 (Residues: 21-115; Coverage: 100%)
Gene names: Gm16848, Igkv12-41
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Ig heavy chain V region PJ14 Chain: B
Molecule details ›
Chain: B
Length: 116 amino acids
Theoretical weight: 12.86 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01820 (Residues: 20-115; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Lysozyme C Chain: C
Molecule details ›
Chain: C
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
Expression system: Not provided
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
Spacegroup: C2
Unit cell:
a: 129.2Å b: 60.8Å c: 56.9Å
α: 90° β: 119.3° γ: 90°
R-values:
R R work R free
0.185 0.185 not available
Expression systems:
  • Escherichia coli
  • Not provided