5YDH

Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector anopheles gambiae, 3.2 A

Summary for 5YDH

• Entry DOI: 10.2210/pdb5ydh/pdb
• Related: 5X61
• Descriptor: Acetylcholinesterase, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: alpha/beta hydrolase, hydrolase
• Biological source: Anopheles gambiae (African malaria mosquito)
• Cellular location: Cell junction, synapse: Q869C3
• Total number of polymer chains: 2
• Total formula weight: 134495.41

Authors

Han, Q.,Guan, H.,Robinson, H.,Ding, H.,Liao, C.,Li, J. (deposition date: 2017-09-13, release date: 2018-03-07, Last modification date: 2024-11-06)

• Primary citation: Han, Q.,Guan, H.,Ding, H.,Liao, C.,Robinson, H.,Li, J.; Crystal structures of acetylcholinesterase of the malaria vector Anopheles gambiae reveal a polymerization interface, ligand binding residues and post translational modifications; To Be Published,

Experimental method

X-RAY DIFFRACTION (3.21 Å)