Figure 5: Cphy117820–462 active site architecture. | Scientific Reports

Figure 5: Cphy117820–462 active site architecture.

From: Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans

Figure 5

(A) Surface slice through Cphy117820–462 showing the position of NAD+ and modelled hexanal substrate. Protein residues and substrates shown as stick representations with different coloured carbon atoms, the active-site histidine is shown in red for clarity. The ligand/substrate-binding tunnel is open at both ends and accommodates the NAD+/CoA cofactors at one end and the aldehyde ligand at the other. The aldehyde-binding portion of the tunnel is lined with hydrophobic residues and is gated by F423, which is present in multiple conformations in the crystal structure. (B) Binding of CoA in the active site showing distances between H387 and C269 and the sulphur of the CoA and E357. CoA shown in magenta.

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