› 1di4

X-ray diffraction
2Å resolution

ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME

Released:
DOI: 10.2210/pdb1di4/pdb
PDB entry 1di4 coloured by chain, front view.
PDB entry 1di4 coloured by chain, side view.
PDB entry 1di4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of amino acid residues at turns in the conformational stability and folding of human lysozyme.
Takano K, Yamagata Y, Yutani K
Biochemistry 39 8655-65 (2000)
PMID: 10913274

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: 128 amino acids
Theoretical weight: 14.59 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61626 (Residues: 19-148; Coverage: 99%)
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: 45.8Å b: 59.27Å c: 38.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.165 not available
Expression system: Saccharomyces cerevisiae

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Citations

1 review citation

Lysozyme and Its Application as Antibacterial Agent in Food Industry.
Nawaz et al. (2022)
28 other articles