Structure analysis

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT

X-ray diffraction
1.8Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7000 Å2
Buried surface area: 0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): 0 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 130 amino acids
Theoretical weight: 14.69 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61626 (Residues: 19-147; Coverage: 99%)
Gene names: LYZ, LZM
Pfam: C-type lysozyme/alpha-lactalbumin family
InterPro:
CATH: Lysozyme
SCOP: C-type lysozyme

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