› 1gfk

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

Released:
DOI: 10.2210/pdb1gfk/pdb
PDB entry 1gfk coloured by chain, front view.
PDB entry 1gfk coloured by chain, side view.
PDB entry 1gfk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability.
Funahashi J, Takano K, Yamagata Y, Yutani K
J Biol Chem 277 21792-800 (2002)
PMID: 11927576

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 Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 14.74 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 NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 56.35Å b: 61.34Å c: 32.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.163 not available
Expression system: Saccharomyces cerevisiae

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Citations

1 review citation

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
6 other articles