The NADPH binding site on beef liver catalase.

The NADPH binding site on beef liver catalase.

Fita, I.,  Rossmann, M.G.

Journal: (1985) Proc.Natl.Acad.Sci.USA 82: 1604-1608

PubMed: 3856839  

Figure 1.  Catalase  (PDB_ID: 8CAT) imported into Sketchfab.

PubMed Abstract:

Beef liver and human erythrocyte catalases (EC bind NADP tenaciously [Kirkman, H. N. & Gaetani, G. F. (1984) Proc.Natl. Acad. Sci. USA 81, 4343-4348]. The position of NADP on beef liver catalase corresponds to the carboxyl-terminal polypeptidehinge in Penicillium vitale fungal catalase, which connects the common catalase structure to the additional flavodoxin-like domain.In contrast to nearly all other known structures of protein-bound NADP, NAD, and FAD, the NADP molecule of beef liver catalase isfolded into a right-handed helix and bound, in part, in the vicinity of the carboxyl end of two alpha-helices. A water molecule (W7)occupies a pseudosubstrate site close to the C4 position of the nicotinamide and is hydrogen bonded to His-304. Although theNADP and heme groups approach each other to within 13.7 A, there is no direct interaction. The function of the NADP remains amystery.

Animals, Binding Sites, Catalase, Cattle, Liver, Molecular Conformation, NADP, Protein ConformationRelated Structures:
Primary Citation of:  7CAT   8CAT

Annotating Proteins & Embedding onto websites with Sketchfab

Catalase (PDB_ID: 8CAT) was imported in Sketchfab (SF) using standard methods.  The protein subunits were separated in 3DS Max and exported using Sketchfab’s 3DS Max Plugin.

Once the protein was imported into SF, lighting and background image were adjusted.  Using the built-in annotation feature, positions on the structure were marked. The generated embed code was copied and pasted onto this page (see Fig. 1).  Click the “Play” button to start the interactivity.

Use the arrows located on the bottom of the viewer ( arows) to navigate to the various positions!

The ability to embed interactive protein structures directly into websites may be very useful for online scientific publications.