1TMN
Binding of n-carboxymethyl dipeptide inhibitors to thermolysin determined by x-ray crystallography. a novel class of transition-state analogues for zinc peptidases
Summary for 1TMN
Entry DOI | 10.2210/pdb1tmn/pdb |
Related PRD ID | PRD_000380 |
Descriptor | THERMOLYSIN, N-[(1R)-1-carboxy-3-phenylpropyl]-L-leucyl-L-tryptophan, CALCIUM ION, ... (5 entities in total) |
Functional Keywords | 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 | 35067.59 |
Authors | Monzingo, A.F.,Matthews, B.W. (deposition date: 1987-06-29, release date: 1989-01-09, Last modification date: 2024-05-22) |
Primary citation | Monzingo, A.F.,Matthews, B.W. Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases Biochemistry, 23:5724-5729, 1984 Cited by PubMed: 6395881DOI: 10.1021/bi00319a010 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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