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Structure paper

TitleContribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants.
Journal, issue, pagesBiochemistry, Vol. 37, Page 9355-9362, Year 1998
Publish dateFeb 9, 1998 (structure data deposition date)
AuthorsYamagata, Y. / Kubota, M. / Sumikawa, Y. / Funahashi, J. / Takano, K. / Fujii, S. / Yutani, K.
External linksBiochemistry / PubMed:9649316
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-1wqm:
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1wqn:
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1wqo:
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1wqp:
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1wqq:
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1wqr:
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / HYDROLASE (O-GLYCOSYL) / GLYCOSIDASE / BACTERIOLYTIC ENZYME

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