2FJK
Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus
Summary for 2FJK
Entry DOI | 10.2210/pdb2fjk/pdb |
Descriptor | Fructose-bisphosphate aldolase, 1,3-DIHYDROXYACETONEPHOSPHATE (3 entities in total) |
Functional Keywords | beta-alpha-barrels, lyase |
Biological source | Thermus caldophilus |
Total number of polymer chains | 4 |
Total formula weight | 134324.51 |
Authors | Lee, J.H.,Im, Y.J.,Rho, S.-H.,Kim, M.-K.,Kang, G.B.,Eom, S.H. (deposition date: 2006-01-03, release date: 2006-08-08, Last modification date: 2011-07-13) |
Primary citation | Lee, J.H.,Bae, J.,Kim, D.,Choi, Y.,Im, Y.J.,Koh, S.,Kim, J.S.,Kim, M.-K.,Kang, G.B.,Hong, S.-I.,Lee, D.-S.,Eom, S.H. Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus Biochem.Biophys.Res.Commun., 347:616-625, 2006 Cited by PubMed: 16843441DOI: 10.1016/j.bbrc.2006.06.139 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report