1ic5

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD99A)-HEN LYSOZYME COMPLEX

Released:
Model geometry
Fit model/data
Data not deposited

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-132836 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Immunoglobulin kappa variable 5-48 Chain: L
Molecule details ›
Chain: L
Length: 107 amino acids
Theoretical weight: 11.62 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01642 (Residues: 21-115; Coverage: 100%)
Gene names: Gm10881, Igkv5-48
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Ig heavy chain V region 36-60 Chain: H
Molecule details ›
Chain: H
Length: 114 amino acids
Theoretical weight: 12.75 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01823 (Residues: 1-113; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Lysozyme C Chain: Y

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MACSCIENCE
Spacegroup: P41212
Unit cell:
a: 57.001Å b: 57.001Å c: 238.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.165 0.252
Expression system: Escherichia coli BL21(DE3)