› 1b5u

X-ray diffraction
1.8Å resolution

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT

Released:
DOI: 10.2210/pdb1b5u/pdb
PDB entry 1b5u coloured by chain, front view.
PDB entry 1b5u coloured by chain, side view.
PDB entry 1b5u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants.
Takano K, Yamagata Y, Kubota M, Funahashi J, Fujii S, Yutani K
Biochemistry 38 6623-9 (1999)
PMID: 10350481

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: 14.7 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: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P212121
Unit cell:
a: 56.96Å b: 60.98Å c: 33.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 not available
Expression system: Saccharomyces cerevisiae

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Citations

3 review citations

Differential scanning calorimetry techniques: applications in biology and nanoscience.
Gill et al. (2010)
2 more