4KAP

The Binding of Benzoarylsulfonamide Ligands to Human Carbonic Anhydrase is Insensitive to Formal Fluorination of the Ligand

Summary for 4KAP

• Entry DOI: 10.2210/pdb4kap/pdb
• Descriptor: Carbonic anhydrase 2, ZINC ION, 4,5,6,7-tetrafluoro-1,3-benzothiazole-2-sulfonamide, ... (4 entities in total)
• Functional Keywords: alpha beta, lyase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P00918
• Total number of polymer chains: 1
• Total formula weight: 29331.31

Authors

Lange, H.,Lockett, M.R.,Breiten, B.,Heroux, A.,Sherman, W.,Rappoport, D.,Yau, P.O.,Snyder, P.W.,Whitesides, G.M. (deposition date: 2013-04-22, release date: 2013-07-10, Last modification date: 2024-02-28)

Primary citation

Lockett, M.R.,Lange, H.,Breiten, B.,Heroux, A.,Sherman, W.,Rappoport, D.,Yau, P.O.,Snyder, P.W.,Whitesides, G.M.
The Binding of Benzoarylsulfonamide Ligands to Human Carbonic Anhydrase is Insensitive to Formal Fluorination of the Ligand.
Angew.Chem.Int.Ed.Engl., 52:7714-7717, 2013

PubMed Abstract: It's the water that matters. Pairs of benzo- and perfluorobenzoarylsulfonamide ligands bind to human carbonic anhydrase with a conserved binding geometry, an enthalpy-driven binding, and indistinguishable binding affinities (see picture). These data support the pervasive theory that the lock-and-key model disregards an important component of binding: the water, which fills the binding pocket of the protein and surrounds the ligand.

PubMed: 23788494
DOI: 10.1002/anie.201301813

Experimental method

X-RAY DIFFRACTION (1.45 Å)