 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](us5093fig4mag.jpg)
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Figure 4
Close-up view of the cofactor-binding sites. (a) Residues interacting with the cofactor. The corresponding 2Fo − Fc electron-density maps of the cofactor and Lys274 are shown and contoured at 1.0σ. The cofactor in subunit A is PMP. The cofactor in subunit B is a mixture of PMP and PLP. Lys274 has multiple conformations in each monomer. (b) Interactions between Lys274 and the cofactor, Trp68 and Tyr306*. Hydrogen bonds are depicted as black dotted lines. Distances between the N atom of Lys274 and the C-4′ atom of the cofactor are depicted as red dotted lines. Distances in Å are displayed in red. The asterisk indicates the residue from the neighbouring subunit. |
![[Figure 4]](us5093fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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