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5WG7

Human Carbonic Anhydrase II complexed with AceK

Summary for 5WG7
Entry DOI10.2210/pdb5wg7/pdb
DescriptorCarbonic anhydrase 2, Acesulfame, ZINC ION, ... (5 entities in total)
Functional Keywordscarbonic anhydrase, acesulfame, inhibitor, lyase
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm : P00918
Total number of polymer chains1
Total formula weight30253.24
Authors
Murray, A.B.,Lomelino, C.L.,Supuran, C.T.,McKenna, R. (deposition date: 2017-07-13, release date: 2018-02-07, Last modification date: 2024-03-13)
Primary citationMurray, A.B.,Lomelino, C.L.,Supuran, C.T.,McKenna, R.
"Seriously Sweet": Acesulfame K Exhibits Selective Inhibition Using Alternative Binding Modes in Carbonic Anhydrase Isoforms.
J. Med. Chem., 61:1176-1181, 2018
Cited by
PubMed Abstract: Human carbonic anhydrase IX (CA IX) is upregulated in neoplastic tissues; as such, it is studied as a drug target for anticancer chemotherapy. Inhibition of CA IX has been shown to be therapeutically favorable in terms of reducing tumor growth. Previously, saccharin, a commonly used artificial sweetener, has been observed to selectively inhibit CA IX over other CA isoforms. In this study, X-ray crystallography showed acesulfame potassium (Ace K) binding directly to the catalytic zinc in CA IX (mimic) and through a bridging water in CA II. This modulation in binding is reflected in the binding constants, with Ace K inhibiting CA IX but not other CA isoforms. Hence, this study establishes the potential of Ace K (an FDA approved food additive) as a lead compound in the design and development of CA IX specific inhibitors.
PubMed: 29266943
DOI: 10.1021/acs.jmedchem.7b01470
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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