ISDA: 4KAP

Deposition Date 2013-04-22

Release Date 2013-07-10

Last Version Date 2024-02-28

Entry Detail

PDB ID:

4KAP

Keywords:

LYASE

Title:

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

Biological Source:

Source Organism(s):

Homo sapiens (Taxon ID: 9606)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.45 Å

R-Value Free:

0.22

R-Value Work:

0.19

R-Value Observed:

0.19

Space Group:

P 1 21 1

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Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Carbonic anhydrase 2
Gene (Uniprot):CA2
Chain IDs:A
Chain Length:258
Number of Molecules:1
Biological Source:Homo sapiens

UniProt ID:P00918 Pfam ID:PF00194 EC:4.2.1.1

Ligand Molecules

1QV

Primary Citation

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

Lockett, M.R, Lange, H, Breiten, B, Heroux, A, Sherman, W, Rappoport, D, Yau, P.O, Snyder, P.W, Whitesides, G.M.Show

Angew. Chem. Int. Ed. Engl. 52 7714 7717 (2013)

PMID: 23788494 DOI: 10.1002/anie.201301813

Abstact

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.

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Primary Citation of related structures

Abstact

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