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CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

X-ray diffraction
1.8Å resolution
PDB entry 1yaq coloured by chain, front view.
PDB entry 1yaq coloured by chain, side view.
PDB entry 1yaq coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Lysozyme C
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Multimeric state: monomeric
Accessible surface area: 6738.45 Å2
Buried surface area: 131.9 Å2
Dissociation area: 65.95 Å2
Dissociation energy (ΔGdiss): 13.43 kcal/mol
Dissociation entropy (TΔSdiss): -1.11 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158303

Macromolecules

Lysozyme C
Chain: A
Length: 130 amino acids
Theoretical weight: 14.71 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61626 (Residues: 19-148; Coverage: 100%)
Gene names: LYZ, LZM
Pfam: C-type lysozyme/alpha-lactalbumin family
InterPro:
CATH: Lysozyme
SCOP: C-type lysozyme
Lysozyme C in PDB entry 1yaq, assembly 1, front view.
Lysozyme C in PDB entry 1yaq, assembly 1, side view.
Lysozyme C in PDB entry 1yaq, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P61626  
1130102030405060708090100110120130
 
50100
UniProt
P61626
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Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
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