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. Author manuscript; available in PMC: 2023 Jan 25.
Published in final edited form as: Cell Rep. 2022 Dec 27;41(13):111876. doi: 10.1016/j.celrep.2022.111876

Figure 1. Structure of bovine GAPDH.

Figure 1.

(A) Cryo-EM map of GAPDH.

(B) Structure of GAPDH. GAPDH forms a tetramer with D2 symmetry. In both (A) and (B), protomers are distinguished by individual colors.

(C) Layout of a GAPDH subunit, which can be divided into two domains, N-terminal domain (blue) and C-terminal domain (red). A single NAD+ ligand is identified in each subunit of the GAPDH tetramer (orange sticks).

(D) Zoomed view of the NAD+-binding site. NAD+ is depicted as orange sticks, cryo-EM density of NAD+ (3σ) is shown as orange mesh, and residues within 4 Å of bound NAD+ are shown as gray sticks.