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4TMN

SLOW-AND FAST-BINDING INHIBITORS OF THERMOLYSIN DISPLAY DIFFERENT MODES OF BINDING. CRYSTALLOGRAPHIC ANALYSIS OF EXTENDED PHOSPHONAMIDATE TRANSITION-STATE ANALOGUES

Summary for 4TMN
Entry DOI10.2210/pdb4tmn/pdb
Related5TMN
Related PRD IDPRD_000656
DescriptorTHERMOLYSIN, N-[(S)-[(1R)-1-{[(benzyloxy)carbonyl]amino}-2-phenylethyl](hydroxy)phosphoryl]-L-leucyl-L-alanine, CALCIUM ION, ... (5 entities in total)
Functional Keywordshydrolase-hydrolase inhibitor complex, metalloproteinase, hydrolase/hydrolase inhibitor
Biological sourceBacillus thermoproteolyticus
Cellular locationSecreted: P00800
Total number of polymer chains1
Total formula weight35107.55
Authors
Holden, H.M.,Tronrud, D.E.,Monzingo, A.F.,Weaver, L.H.,Matthews, B.W. (deposition date: 1987-06-29, release date: 1989-01-09, Last modification date: 2022-11-23)
Primary citationHolden, H.M.,Tronrud, D.E.,Monzingo, A.F.,Weaver, L.H.,Matthews, B.W.
Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.
Biochemistry, 26:8542-8553, 1987
Cited by
PubMed: 3442675
DOI: 10.1021/bi00400a008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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