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; PubMed: 24914980; DOI: 10.1107/S1399004714007664

Experimental method

X-RAY DIFFRACTION (2.6 Å)