› 1g7h

X-ray diffraction
1.85Å resolution

CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXED WITH THE MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1.3(VLW92A)

Released:
DOI: 10.2210/pdb1g7h/pdb
PDB entry 1g7h coloured by chain, front view.
PDB entry 1g7h coloured by chain, side view.
PDB entry 1g7h coloured by chain, top view.
Source organisms:
Primary publication:
Estimation of the hydrophobic effect in an antigen-antibody protein-protein interface.
Sundberg EJ, Urrutia M, Braden BC, Isern J, Tsuchiya D, Fields BA, Malchiodi EL, Tormo J, Schwarz FP, Mariuzza RA
Biochemistry 39 15375-87 (2000)
PMID: 11112523

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)
PDBe Complex ID:
PDB-CPX-224916 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
ANTI-HEN EGG WHITE LYSOZYME MONOCLONAL ANTIBODY D1.3 Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.59 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
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
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: SIEMENS
Spacegroup: C2
Unit cell:
a: 128.05Å b: 60.42Å c: 56.16Å
α: 90° β: 119.26° γ: 90°
R-values:
R R work R free
0.203 0.203 not available
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Protein-protein interaction and quaternary structure.
Janin et al. (2008)
8 more

3 mentions without citation

An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state.
Zhang et al. (2004)
2 more