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Literature summary for 4.3.2.10 extracted from
- Structure of HisF, a histidine biosynthetic protein from Pyrobaculum aerophilum (2001), Acta Crystallogr. Sect. D, 57, 1518-1525 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Pyrobaculum aerophilum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the structure is determined by molecular replacement and refined at 2.0 A resolution to a crystallographic R factor of 20.6% and a free R of 22.7%. The structure adopts a classic (beta/alpha)8 barrel fold and has networks of surface salt bridges that may contribute to thermostability | Pyrobaculum aerophilum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrobaculum aerophilum | Q8ZY16 AND Q8ZY40 | Q8ZY16: subunit HisF, Q8ZY40: subunit HisH | - |
| Pyrobaculum aerophilum DSM 7523 | Q8ZY16 AND Q8ZY40 | Q8ZY16: subunit HisF, Q8ZY40: subunit HisH | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrobaculum aerophilum |
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Release 2023.1 (January 2023)
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