8AA6

CAII in complex with meta-carboran-propylsulfonamid

Summary for 8AA6

• Entry DOI: 10.2210/pdb8aa6/pdb
• Related: 6YZT
• Descriptor: Carbonic anhydrase 2, ZINC ION, meta-carboran-propylsulfonamid, ... (4 entities in total)
• Functional Keywords: inhibitor, complex, carbonicanhydrase, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 29608.77

Authors

Brynda, J.,Rezacova, P.,Kugler, M. (deposition date: 2022-06-30, release date: 2023-05-10, Last modification date: 2024-02-07)

Primary citation

Fanfrlik, J.,Brynda, J.,Kugler, M.,Lepsik, M.,Pospisilova, K.,Holub, J.,Hnyk, D.,Nekvinda, J.,Gruner, B.,Rezacova, P.
B-H⋯ pi and C-H⋯ pi interactions in protein-ligand complexes: carbonic anhydrase II inhibition by carborane sulfonamides.
Phys Chem Chem Phys, 25:1728-1733, 2023

PubMed Abstract: Among non-covalent interactions, B-H⋯π and C-H⋯π hydrogen bonding is rather weak and less studied. Nevertheless, since both can affect the energetics of protein-ligand binding, their understanding is an important prerequisite for reliable predictions of affinities. Through a combination of high-resolution X-ray crystallography and quantum-chemical calculations on carbonic anhydrase II/carborane-based inhibitor systems, this paper provides the first example of B-H⋯π hydrogen bonding in a protein-ligand complex. It shows that the B-H⋯π interaction is stabilized by dispersion, followed by electrostatics. Furthermore, it demonstrates that the similar C-H⋯π interaction is twice as strong, with a slightly smaller contribution of dispersion and a slightly higher contribution of electrostatics. Such a detailed insight will facilitate the rational design of future protein ligands, controlling these types of non-covalent interactions.

PubMed: 36594655
DOI: 10.1039/d2cp04673c

Experimental method

X-RAY DIFFRACTION (1.15 Å)