view article

Figure 2
Structure of HinfPDH. (a) Ribbon diagram of a HinfPDH monomer complexed with NAD+ and a tyrosine molecule. Helices α1–α12 and strands β1–β7 are indicated. The C-terminal domain is colored green and the helices and β-strands of the N-terminal domain are colored cyan and red, respectively. Bound tyrosine and NAD+ molecules are shown in ball-and-stick representation; C, O, N and phosphate atoms are colored yellow, red, blue and orange, respectively. (b) Ribbon diagram of the HinfPDH dimer; monomer A is colored green and monomer B is colored orange. Helices are shown as cylinders. (c) Top view compared with (b) of the HinfPDH dimer. (d) Diagram showing the secondary-structure elements of HinfPDH superimposed on its primary sequence. The labeling of secondary-structure elements is in accord with PDBsum (https://www.ebi.ac.uk/pdbsum ), where α-helices (H1–H12) and β-strands (β1–β7) are sequentially labeled, β-turns and γ-turns are designated by Greek letters (β, γ) and β-hairpins are indicated by red loops.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds