5WLY

E. coli LpxH- 8 mutations

Summary for 5WLY

• Entry DOI: 10.2210/pdb5wly/pdb
• Descriptor: UDP-2,3-diacylglucosamine hydrolase, MANGANESE (II) ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: lipid a synthesis, open conformation, udp-diacyl-glucosamine pyrophosphohydrolase, apha/beta-hydrolase, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 27985.40

Authors

Bohl, T.E.,Aihara, H.,Shi, K.,Lee, J.K. (deposition date: 2017-07-28, release date: 2018-04-11, Last modification date: 2023-10-04)

• Primary citation: Bohl, T.E.,Ieong, P.,Lee, J.K.,Lee, T.,Kankanala, J.,Shi, K.,Demir, O.,Kurahashi, K.,Amaro, R.E.,Wang, Z.,Aihara, H.; The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release.; J. Biol. Chem., 293:7969-7981, 2018; PubMed: 29626094; DOI: 10.1074/jbc.RA118.002503

Experimental method

X-RAY DIFFRACTION (2 Å)