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Literature summary extracted from

  • Battula, P.; Dubnovitsky, A.P.; Papageorgiou, A.C.
    Structural basis of L-phosphoserine binding to Bacillus alcalophilus phosphoserine aminotransferase (2013), Acta Crystallogr. Sect. D, 69, 804-811.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.52 in presence or absence of L-phosphoserine, to resolutions of 1.5 and 1.6 A, respectively. Substrate binding induces local conformational changes. No domain or subunit movements are observed. Residues Arg42 and Arg328 and His41 and His327 form a tight binding site for the phosphate group of L-phosphoserine Alkalihalobacillus alcalophilus

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.52 Alkalihalobacillus alcalophilus Q9RME2
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Synonyms

EC Number Synonyms Comment Organism
2.6.1.52 serC
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Alkalihalobacillus alcalophilus