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Literature summary for 3.4.21.50 extracted from

  • Ohnishi, Y.; Masaki, T.; Yamada, T.; Kurihara, K.; Tanaka, I.; Niimura, N.
    A preliminary neutron diffraction analysis of Achromobacter protease I (2010), J. Phys. Conf. Ser., 251, 012032.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A Achromobacter lyticus

Organism

Organism UniProt Comment Textmining
Achromobacter lyticus
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Achromobacter lyticus M497-1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A Achromobacter lyticus ?
-
?
additional information neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A Achromobacter lyticus M497-1 ?
-
?