› 1ioc

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T

Released:
DOI: 10.2210/pdb1ioc/pdb
PDB entry 1ioc coloured by chain, front view.
PDB entry 1ioc coloured by chain, side view.
PDB entry 1ioc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme.
Goda S, Takano K, Yamagata Y, Maki S, Namba K, Yutani K
J Biochem 132 655-61 (2002)
PMID: 12359083

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: 134 amino acids
Theoretical weight: 15.11 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
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 3 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P6122
Unit cell:
a: 90.12Å b: 90.12Å c: 92.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 not available
Expression system: Komagataella pastoris

Quick links

Citations

3 citation in other articles

Characterization of oligomeric species on the aggregation pathway of human lysozyme.
Frare et al. (2009)
2 more