8TLN
STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS
Replaces: 3TLNReplaces: 1TLNReplaces: 2TLNSummary for 8TLN
Entry DOI | 10.2210/pdb8tln/pdb |
Descriptor | THERMOLYSIN, VALINE, LYSINE, ... (7 entities in total) |
Functional Keywords | hydrolase(metalloproteinase) |
Biological source | Bacillus thermoproteolyticus |
Cellular location | Secreted: P00800 |
Total number of polymer chains | 1 |
Total formula weight | 34930.50 |
Authors | Tronrud, D.,Matthews, B.W. (deposition date: 1993-09-01, release date: 1994-04-30, Last modification date: 2024-02-14) |
Primary citation | Holland, D.R.,Tronrud, D.E.,Pley, H.W.,Flaherty, K.M.,Stark, W.,Jansonius, J.N.,McKay, D.B.,Matthews, B.W. Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochemistry, 31:11310-11316, 1992 Cited by PubMed: 1445869DOI: 10.1021/bi00161a008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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