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Literature summary extracted from
- Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease (2013), J. Synchrotron Radiat., 20, 933-937.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.B56 | hanging-drop vapor diffusion method, crystallization of the catalytically inactive mutants S97A and K138A of 1510-N in complex with three kinds of substrate peptides of p-stomatin (234NVIVLMLPME243, 232KSNVIVLML240 and 238LMLPMEMLK246), structural analysis | Pyrococcus horikoshii |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.B56 | membrane | - |
Pyrococcus horikoshii | 16020 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.B56 | Pyrococcus horikoshii | O59179 | N-terminal region of open reading frame, PH1510 (residues 16236, designated as 1510-N) is a serine protease | - |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.B56 | PH1510 | - |
Pyrococcus horikoshii |
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Release 2023.1 (January 2023)
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