S-ribosylhomocysteine binds in a deep pocket with the ribose moiety adjacent to the enzyme-bound zinc ion.
For both complexes, the SAM cofactor is bound in a deep pocket located at the edge of the central β-sheet between strands 2, 3 and 4 (Fig. 1b).
In the structure of the human CMTr1 determined in the present study and in the theoretical model of CMTr2, m7G is bound in a deep pocket, but the sugar edge of the nucleoside residue is directed towards the pocket floor, with the methyl group exposed and involved in few interactions with the protein (Fig. 6d).
In the resultant ThyX-NADP+ binary complex, the AMP moiety is bound in a deep pocket similar to that of the same moiety of FAD in the ternary complex, while the nicotinamide part of NADP+ is engaged in a limited number of contacts with ThyX.
In the inward-facing protomers B and B', citrate binds in a deep cytoplasmic cavity.
The UDP-Glc is bound in a deep cleft located at the center of the catalytic domain that consists of highly conserved residues.
The active site is located on the concave side of the β-sheet with ATP bound in a deep pocket at one end of the sheet.
In the complex, NADPH binds in a deep cleft formed by the C-terminus of the parallel β-sheet and helices α4, α5, α6, and α7 burying ∼650 Å of solvent accessible area.
Pyridoxal-phosphate binds in a deep pocket within one subunit, with D160 interacting with the pyridine ring nitrogen and increasing its electron-sink character as is typical in this family of aminotransferases.
The testimony is often fascinating, and the stories are gripping, in particular the grim Albanian situation, a land dispute between neighbors bound up in a deep and ancient code of honor and vengeance.
