 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](aso5001fig3mag.jpg)
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Figure 3
Coenzyme-binding site. The electron density (2Fo − Fc, contoured at 1.5σ) around the NADP+ cofactor (a) is well resolved and clearly matches NADP+ (NADP in chain A is shown). Several key hydrogen-bonding interactions (b) are made between the Asp14, Arg15 and Arg38 residues of BcSDR and the phosphate moiety of NADP+. Here, C atoms are shown in green, O atoms in red, N atoms in blue and P atoms in orange. As demonstrated by superposition of BcSDR with an NAD-binding SDR (c) (PDB entry 5u8p, shown in pink with pink C atoms), residues (Leu115 and Glu118 of PDB entry 5u8p) of a nearby loop and helix provide a sterically selective force for binding NAD versus NADP. This helix that harbors Glu118 in PDB entry 5u8p is absent in BcSDR and would clash with Arg38. Note that further details about the goodness of fit of the coenzyme, including additional maps and images, can be found in the PDB validation report for PDB entry 5u4s. |
![[Figure 3]](aso5001fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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