› 1ip3

X-ray diffraction
1.8Å resolution

G68A HUMAN LYSOZYME

Released:
DOI: 10.2210/pdb1ip3/pdb
PDB entry 1ip3 coloured by chain, front view.
PDB entry 1ip3 coloured by chain, side view.
PDB entry 1ip3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein.
Takano K, Yamagata Y, Yutani K
Proteins 45 274-80 (2001)
PMID: 11599030

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
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.73 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

2 bound ligands:
Ligand NA 1 x NA
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P212121
Unit cell:
a: 42.245Å b: 64.321Å c: 111.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Saccharomyces cerevisiae

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Citations

1 review citation

Structural features of thermozymes.
Li et al. (2005)
7 other articles