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The pocket accommodating the side chain of Tyr18 is mainly composed of several hydrophobic residues including Ile23, Lys51 and Leu53 of LC3B, and forms a hydrogen bond between the carbonyl oxygen of LC3B and19 and the hydroxyl group of FUNDC1 Tyr18 (Fig. 3A).
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This subsite accommodates the side chain of BR22, which forms a direct hydrogen bond with the hydroxyl group of TY60A.
In the ligand-complex the pocket accommodates the side chain of a key anchor residue of the peptide (Fig. 1A).
The amino acid side chain of a mutant at this position would point into a hydrophobic niche that also accommodates the side chain of L574 from another monomer.
It is located within the peptide binding site and accommodates the side chain of a key-anchor residue of the peptide ligand.
The P1 pocket in the DR4 binding site that accommodates the side chain of Phe263 in 1 is a large, deep and mainly lipophilic pocket (Figure 2b).
Class II molecules have polymorphic pockets that accommodate the side chains of bound peptides.
FVIIa recognizes PAR-2 predominantly by catalytic cleft interactions, while the S2' pocket accommodates the side chain of PAR-2 L, P2' [ 84].
This residue is part of an extended hydrophobic groove of the REM domain that accommodates the side chains of two hydrophobic residues (Ile956 and Phe958) of the helical hairpin of the CDC25 domain.
RosettaDock uses a low resolution Monte Carlo search and backbone optimization algorithm to optimally position a submitted monomer pair, followed by a refinement to relax the backbone and accommodate the side chains (Gray et al. 2003).
RosettaDock is a server that uses a low-resolution Monte Carlo search and backbone optimization algorithm to position the submitted chain pair, followed by a refinement to relax the backbone and accommodate the side chains (Gray et al. 2003).
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