The phrase "a pocket that accommodates" is correct and usable in written English.
It can be used to describe a pocket designed to hold or fit certain items comfortably.
Example: "This jacket features a pocket that accommodates a smartphone, ensuring it stays secure while you move."
Alternatives: "a pocket that fits" or "a pocket that holds".
The nicotinamide ring has more interactions with the enzyme than does the benzyl alcohol, which is located in a hydrophobic pocket that accommodates a variety of alcohols.
The 10mer remodels the binding site, so that the P2 Glu interacts with Asp24 that also interacts with Arg9 in a so-called charge transfer mechanism, creating a hydrophobic pocket that accommodates Pc-2 Leu (and Pc Val fits in the hydrophobic pocket).
MUPs belong to the lipocalin superfamily, whose conserved structure is a β-barrel made of eight antiparallel β-strands forming a hydrophobic pocket that accommodates small organic molecules.
The Rho GTPases RhoA, Rac1, and Cdc42 are posttranslationally modified by a 20-carbon geranylgeranyl lipid and are solubilized from membranes and sequestered in the cytosol in an inactive state by binding to RhoGDIs, which have a hydrophobic pocket that accommodates the geranylgeranyl group (Hoffman et al., 2000).
Overall, this region of the Mhp1 protein forms a hydrophobic pocket that accommodates the indole moiety of the hydantoin as shown in the surface representation in Fig 1C.
As shown in Figure 1B and C, a perfect pocket that accommodates the C6 group of the sugar in position -1 was recognized together with a pocket for the sugar in position 1.
Compared with the structure of TIS11D, the characteristic KTEL V) motif at the N-terminus of each zinc finger domain provides a critical part of the RNA-binding surface; each motif forms two walls of a deep pocket that accommodates the bases of U6 and U2 in fingers 1 and 2, respectively.
This is achieved by a hydrophobic pocket that accommodates the methionine residue (M in MEEVD) from Hsp90 and the isoleucine residue (I in IEEVD) of human Hsp70 and in doing so twists the upstream peptide, which differs between the two chaperones, and hoists it clear of the TPR-domain groove [ 24].
Mup proteins form a characteristic glove shape, encompassing a ligand-binding pocket that accommodates specific small, organic chemicals.
The HEF binding site also contains a unique hydrophobic pocket that accommodates the acetyl methyl group (Rosenthal et al., 1998).
