Structure analysis

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA 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: 6987.13 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158303

Macromolecules

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
Pfam: C-type lysozyme/alpha-lactalbumin family
InterPro:
CATH: Lysozyme
SCOP: C-type lysozyme
PDBe-KB: UniProt Coverage View: P61626  
1130102030405060708090100110120130
 
50100
UniProt
P61626
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions

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