› 1i22

X-ray diffraction
1.8Å resolution

MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)

Released:
DOI: 10.2210/pdb1i22/pdb
PDB entry 1i22 coloured by chain, front view.
PDB entry 1i22 coloured by chain, side view.
PDB entry 1i22 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and thermodynamic responses of mutations at a Ca2+ binding site engineered into human lysozyme.
Kuroki R, Yutani K
J Biol Chem 273 34310-5 (1998)
PMID: 9852096

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 130 amino acids
Theoretical weight: 14.81 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61626 (Residues: 19-148; Coverage: 100%)
Gene names: LYZ, LZM
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 62Å b: 113Å c: 41.2Å
α: 90° β: 74.6° γ: 90°
R-values:
R R work R free
0.172 not available not available
Expression system: Saccharomyces cerevisiae

Quick links

Citations

2 review citations

Electrolytes in biomolecular systems studied with the 3D-RISM/RISM theory.
Maruyama et al. (2011)
1 more