 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](tb5173fig3mag.jpg)
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Figure 3
PxSDR superposed on its closest structural orthologues reveals differences in the substrate- and cofactor-binding cavities. (a) The substrate-binding cavities of the proteins, indicated in the blue circle, have differences that are indicative of different substrate specificities. (b) PxSDR in black has a unique loop insertion in the cofactor-binding cavity, while the other proteins have a well conserved cofactor-binding cavity and loops. The superposed structures are PDB entry 5jc8 (apo structure of PxSDR, black), PDB entry 1iy8 (crystal structure of levodione reductase from Leifsonia aquatica, red), PDB entry 3ftp [3-ketoacyl-(acyl-carrier-protein) reductase from Burkholderia pseudomallei, yellow], PDB entry 6t6n [Klebsiella pneumoniae FabG2(NADH-dependent) in complex with NADH, wheat] and PDB entry 6ixm (ketone reductase ChKRED20 from the genome of Chryseobacterium, aquamarine). The cofactor, NADH and substrate, (4R)-2-methylpentane-2,4-diol, are from PDB entry 1iy8. Structures were superposed with PyMOL. |
![[Figure 3]](tb5173fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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