3TMN
THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS
Summary for 3TMN
Entry DOI | 10.2210/pdb3tmn/pdb |
Descriptor | THERMOLYSIN, VALINE, TRYPTOPHAN, ... (6 entities in total) |
Functional Keywords | hydrolase, metalloproteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Bacillus thermoproteolyticus |
Cellular location | Secreted: P00800 |
Total number of polymer chains | 1 |
Total formula weight | 34909.40 |
Authors | Holden, H.M.,Matthews, B.W. (deposition date: 1987-06-29, release date: 1989-01-09, Last modification date: 2024-05-22) |
Primary citation | Holden, H.M.,Matthews, B.W. The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis. J.Biol.Chem., 263:3256-3260, 1988 Cited by PubMed: 3343246PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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