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 Cited by PubMed: 29626094DOI: 10.1074/jbc.RA118.002503 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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