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Thermolysin
From Proteopedia
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**[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br /> | **[[1fjo]], [[1fj3]], [[1fjq]], [[1fjt]], [[1fju]], [[1fjv]], [[1fjw]], [[4tli]], [[5tli]], [[6tli]], [[7tli]], [[8tli]], [[1tli]], [[2tli]], [[3tli]] – TML soaked in organic solvents<br /> | ||
**[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]] – TML residues 233-548+inhibitor<br /> | **[[3fv4]], [[3fxp]], [[3flf]], [[3fb0]], [[3fcq]], [[3f28]], [[3f2p]], [[4mtw]], [[4mwp]], [[4mxj]], [[4mzn]], [[4n4e]], [[4n5p]], [[4n66]], [[4oi5]] – TML residues 233-548+inhibitor<br /> | ||
| - | ** | + | **[[3for]], [[1y3g]], [[1zdp]], [[1z9g]], [[1pes]], [[1pe7]], [[1pe8]], [[1os0]], [[1kto]], [[1ks7]], [[1kro]], [[1kr6]], [[1kkk]], [[1kjo]], [[1kjp]], [[1qf0]], [[1qf1]], [[1qf2]], [[1hyt]], [[1thl]], [[6tmn]], [[7tln]], [[4tln]], [[5tln]], [[1pe5]], [[3ms3]], [[3msa]], [[3msf]], [[3msn]], [[3n21]], [[3nn7]], [[3t73]], [[3t74]], [[3t87]], [[3t8c]], [[3t8d]], [[3t8f]], [[3t8g]], [[3t8h]], [[4h57]], [[4d9w]], [[4d91]] – TML+inhibitor<br /> |
**[[3ssb]] – TML + Impi-α<br /> | **[[3ssb]] – TML + Impi-α<br /> | ||
**[[3t2h]] – TML + trimethylamine oxide<br /> | **[[3t2h]] – TML + trimethylamine oxide<br /> | ||
Revision as of 09:03, 27 November 2016
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3D Structures of Thermolysin
Updated on 27-November-2016
References
- ↑ Matthews, BW. (1988): Structural basis of the action of thermolysin and related zinc peptidases. In: Acc. Chem. Res. 21(9); 333–340; http://dx.doi.org/10.1021/ar00153a003
- ↑ Pelmenschikov V, Blomberg MR, Siegbahn PE. A theoretical study of the mechanism for peptide hydrolysis by thermolysin. J Biol Inorg Chem. 2002 Mar;7(3):284-98. Epub 2001 Sep 27. PMID:11935352 doi:http://dx.doi.org/10.1007/s007750100295

