› 1lz1

X-ray diffraction
1.5Å resolution

REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS

Released:
DOI: 10.2210/pdb1lz1/pdb
PDB entry 1lz1 coloured by chain, front view.
PDB entry 1lz1 coloured by chain, side view.
PDB entry 1lz1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions.
Artymiuk PJ, Blake CC
J Mol Biol 152 737-62 (1981)
PMID: 7334520

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: 14.72 KDa
Source organism: Homo sapiens
Expression system: Not provided
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 57.13Å b: 60.99Å c: 32.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.177 not available
Expression system: Not provided

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Citations

6 review citations

Hydrogen bonding in globular proteins.
Baker et al. (1984)
5 more

36 mentions without citation

Protein-Nanoparticle Interaction: Corona Formation and Conformational Changes in Proteins on Nanoparticles.
Park SJ. (2020)
35 more