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Structure paper

TitleRole of amino acid residues at turns in the conformational stability and folding of human lysozyme.
Journal, issue, pagesBiochemistry, Vol. 39, Page 8655-8665, Year 2000
Publish dateNov 28, 1999 (structure data deposition date)
AuthorsFunahashi, J. / Takano, K. / Yamagata, Y. / Yutani, K.
External linksBiochemistry / PubMed:10913274
MethodsX-ray diffraction
Resolution1.8 - 2.2 Å
Structure data

PDB-1di3:
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1di4:
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1di5:
ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1gaz:
Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / STABILITY / TURN / MUTANT / surface mutant

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