› 3hfm

X-ray diffraction
3Å resolution

STRUCTURE OF AN ANTIBODY-ANTIGEN COMPLEX. CRYSTAL STRUCTURE OF THE HY/HEL-10 FAB-LYSOZYME COMPLEX

Released:
DOI: 10.2210/pdb3hfm/pdb
PDB entry 3hfm coloured by chain, front view.
PDB entry 3hfm coloured by chain, side view.
PDB entry 3hfm coloured by chain, top view.
Source organisms:
Primary publication:
Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex.
Padlan EA, Silverton EW, Sheriff S, Cohen GH, Smith-Gill SJ, Davies DR
Proc Natl Acad Sci U S A 86 5938-42 (1989)
PMID: 2762305

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208271 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HYHEL-10 IGG1 FAB (LIGHT CHAIN) Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.55 KDa
Source organism: Mus musculus
Expression system: Not provided
Structure domains: Immunoglobulins
HYHEL-10 IGG1 FAB (HEAVY CHAIN) Chain: H
Molecule details ›
Chain: H
Length: 215 amino acids
Theoretical weight: 23.32 KDa
Source organism: Mus musculus
Expression system: Not provided
Structure domains: Immunoglobulins
Lysozyme C Chain: Y
Molecule details ›
Chain: Y
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: P212121
Unit cell:
a: 57.468Å b: 118.734Å c: 137.678Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 not available not available
Expression system: Not provided

Quick links

Citations

28 review citations

Conformations of immunoglobulin hypervariable regions.
Chothia et al. (1989)
27 more

40 mentions without citation

Relevant B cell epitopes in allergic disease.
Pomés A. (2010)
39 more