Sentence examples for bound at the substrate from inspiring English sources

In this conformation, it is possible to model a molecule of GTP bound at the substrate site, with most of the substrate-binding and catalytic residues in the same positions as in AC (see Figure 4 of [ 9 ]).

The structure of erbstatin also resembled the styryl pharmacophore found in peptide inhibitors incorporating dehydrophenylalanine in place of tyrosine, further supporting the hypothesis that it bound at the substrate phosphorylation site.

The results showed that the xenobiotics bind at the substrate binding site.

The ubiquitin-like protein NEDD8 enhances CRL activity by inducing dynamics of the complex and activating conformational shift of Rbx E2~Ub to bring ubiquitin in close proximity to the substrate bound at the opposite terminus of the E3 ligase [ 100, 194].

Furthermore, in glutamine synthetase this interaction might indirectly contribute to catalysis via a conserved aspartate from this region that interacts with the substrate bound at the active site and helps in anchoring it there.

The analysis of the simulated bound structures of GSK-3β(p) in this spirit suggests that the phosphorylated substrate bound at the ABS could induce partial activation, similar to bound CDK2, whereas a substrate bound at the ABS could render the kinase less active.

As anticipated, both distances Lys−Glu and Asp−Gly favor a salt bridge and hydrogen bond, respectively, when the substrate was bound at the SBS.

The only structure available with substrate bound at the active site in the catalytically active ferrous state is xcTDO.

To understand the binding and inhibition of estrogen sulfotransferase by BFRs, we obtained crystal structures of SULT1E1 in complex with the product cofactor PAP and three different compounds bound at the active site: the natural substrate (E2), a BFR (TBBPA), and a human BFR metabolite (3-OH-BDE-47) at resolutions of 1.95 Å, 2.0 Å, and 2.05 Å, respectively.

The cross-correlation map of a substrate bound at the ABS exhibits high similarity to the cross-correlation map published by Cheng et al. (30), who analyzed the motions of cAMP-dependent protein kinase (PKA) in complex with a small peptide inhibitor (PDB code 1L3R) (56).

Figure 1(A F) shows the highly conserved location of metals and substrates bound at the active site as well as the spatially conserved metal binding residues in various proteins (See legend for details).