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Structure paper

TitleThe binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 263, Page 3256-3260, Year 1988
Publish dateJun 29, 1987 (structure data deposition date)
AuthorsHolden, H.M. / Matthews, B.W.
External linksPubMed:3343246
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-3tmn:
THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-VAL:
VALINE

ChemComp-TRP:
TRYPTOPHAN

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bacillus thermoproteolyticus (bacteria)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / HYDROLASE / METALLOPROTEINASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX

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