3WGB
Crystal structure of aeromonas jandaei L-allo-threonine aldolase
Summary for 3WGB
Entry DOI | 10.2210/pdb3wgb/pdb |
Related | 3WGC |
Descriptor | L-allo-threonine aldolase, N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE], GLYCINE, ... (4 entities in total) |
Functional Keywords | lyase, pyridoxal-5'-phosphate, threonine aldolase |
Biological source | Aeromonas jandaei |
Total number of polymer chains | 4 |
Total formula weight | 147751.37 |
Authors | Qin, H.M.,Imai, F.L.,Miyakawa, T.,Kataoka, M.,Okai, M.,Ohtsuka, J.,Hou, F.,Nagata, K.,Shimizu, S.,Tanokura, M. (deposition date: 2013-08-03, release date: 2014-07-09, Last modification date: 2024-03-20) |
Primary citation | Qin, H.M.,Imai, F.L.,Miyakawa, T.,Kataoka, M.,Kitamura, N.,Urano, N.,Mori, K.,Kawabata, H.,Okai, M.,Ohtsuka, J.,Hou, F.,Nagata, K.,Shimizu, S.,Tanokura, M. L-allo-Threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity. Acta Crystallogr.,Sect.D, 70:1695-1703, 2014 Cited by PubMed: 24914980DOI: 10.1107/S1399004714007664 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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