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Literature summary for 2.5.1.47 extracted from

  • Heine, A.; Canaves, J.M.; Von Delft, F.; Brinen, L.S.; Dai, X.; Deacon, A.M.; Elsliger, M.A.; Eshaghi, S.; Floyd, R.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Guda, C.; Jaroszewski, L.; Karlak, C.; Klock, H.E.; Koesema, E.; Kovarik, J.S.; Kreusch, A.; Kuhn, P.; Lesley, S.A.; McMullan, D.; McPhillips, T.M.; Miller, M.A.; Miller, M.D.; Morse, A.; Moy, K.; Ouyang, J.; Page, R.; Robb, A.; Rodrigues, K.; Schwarzenbacher, R.; Selby, T.L.; Spraggon, G.; Stevens, R.C.; Van Den Bedem, H.; Velasquez, J.; Vincent, J.; Wang, X.; West, B.; Wolf, G.; Hodgson, K.O.; Wooley, J.; Wilson, I.A.
    Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution (2004), Proteins Struct. Funct. Bioinform., 56, 387-391.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
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Subunits

Subunits Comment Organism
More monomer is composed of 15 helices and 9 beta-strands, it consists of two domains A and B and has a phosphate ligand bound to each domain Thermotoga maritima