Sentence examples for bottom of the binding from inspiring English sources

Earlier X-ray crystal structures of Fab 10F11 showed that tryptophan H104 at the bottom of the binding pocket interacts by π-stacking with the aromatic ring of the substrate.

aL2, which differ mainly in the side-chain conformation of Trp H109 (according to a new consensus nomenclature Kabat residue number H95) in the extremely short (three residues) CDR H3 and the presence or absence of a well-resolved molecule of 2-methyl-pentane-2,4-diol in the bottom of the binding pocket.

The β-Gal of the precursor makes a major contact with the "bottom" of the binding interface, which is stabilized by residue T397, while the Le epitope, the α-1,3/4 Fuc (Le Fuc), contacts with another part of the "bottom" and is stabilized by the other "wall" (S346′, T347′, G348′ and D349′) to support the binding outcomes (Figs. 5D, 6 and 7D).

First (Figure 9A), we used a ligand-sided site point to select for poses with a functional group at the bottom of the binding site acting as both a donor and an acceptor, and forming hydrogen bonds to a backbone carbonyl oxygen on one side of the binding site (Leu 251) and to a backbone nitrogen on the other side of the binding site (Thr 242).

The 6-methyl of the pyrimidine moiety inserts into a pocket at the bottom of the binding cleft that is formed by Tyr34, Met310, Ala205 and Gln230.

At the bottom of the binding pocket, Arg of the recognition helix (α5) forms a salt bridge with Asp of α3; the binding of urate would cause a charge repulsion of Asp in α3 that would in turn displace the DNA recognition helix α5, resulting in attenuated DNA binding.

Selectivity and primer unit size appear to involve the side chains of three residues on the loops close to the dimer interface that constitute the bottom of the substrate binding pocket.

Mapping of the location of this mutation on the structure of MtbHadAB reveals that the mutation is located at the N-terminal end of αHD and lies at the bottom of the flavonoid binding pocket (Fig. 6C).

V134 and V112 are located at the catalytic pocket near the nucleophile residue (D108) and at the bottom of the substrate binding pocket, respectively, while L138, H247, and I253 are located at the access tunnels to the catalytic pocket.

The T854A residue is located at the bottom of the ATP binding site on C-lobe and its side chain is in contact distance of erlotinib or gefitinib.

Cys117 is located at the bottom of the FABP4 binding pocket and is in direct contact with ligands in the crystal structures.