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: 2022-11-23)
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: 6395881 DOI: 10.1021/bi00319a010 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation