2YCE

Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.

Replaces:  1W8R

Summary for 2YCE

• Entry DOI: 10.2210/pdb2yce/pdb
• Related: 1OJX 1OK4 1OK6 1W8S
• Descriptor: FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1, D-MANNITOL-1,6-DIPHOSPHATE (3 entities in total)
• Functional Keywords: lyase, glycolysis
• Biological source: THERMOPROTEUS TENAX
• Total number of polymer chains: 10
• Total formula weight: 290831.96

Authors

Lorentzen, E.,Siebers, B.,Hensel, R.,Pohl, E. (deposition date: 2011-03-14, release date: 2011-04-27, Last modification date: 2023-12-20)

• Primary citation: Lorentzen, E.,Siebers, B.,Hensel, R.,Pohl, E.; Mechanism of the Schiff Base Forming Fructose-1,6-Bisphosphate Aldolase: Structural Analysis of Reaction Intermediates.; Biochemistry, 44:4222-, 2005; PubMed: 15766250; DOI: 10.1021/BI048192O

Experimental method

X-RAY DIFFRACTION (1.93 Å)