Fig. 10: Comparison of human SR structures viewed from N-terminal end of α4 helix. | Communications Biology

Fig. 10: Comparison of human SR structures viewed from N-terminal end of α4 helix.

From: Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase

Fig. 10

a View of the malonate (yellow carbons)/ATP (oranges carbons) hSR complex (6ZSP). SR (green carbons) is shown with side-chains of Ser 84 and Tyr 121 (magenta carbons) highlighted. The second subunit in the dimer is partially visible in the bottom right-hand corner (grey semi-transparent spheres). The side-chain of Ser 83 makes a hydrogen bond (dotted red line) to the malonate and the main-chain NH of His 87 also donates a hydrogen bond to the malonate. The carbonyl oxygen of His 82 is arrowed. b Equivalent view of an XChem A subunit. The carbonyl oxygen of His 82 is arrowed. c Equivalent view of an XChem C subunit. d Superposition of structures from (a), (b) and (c) on the large subunit (Cα traces). L-serine (sticks - yellow carbons) has been modelled on the malonate (thin yellow lines - largely hidden under L-serine).

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