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. 2023 Sep 30;24(19):14785. doi: 10.3390/ijms241914785

Figure 2.

Figure 2

Family and size total structure weight distribution of the unique reports of membrane proteins whose structure has been solved at a resolution better than 3 Å by cryo-EM SPA during the last two years (2021–2022) available in the Protein Data Bank. (A) Family groups of α-helical MPs. Other include a single report for the following families: Adventitious MPs/α -helical pore-forming toxins; Bacterial rhodopsin; Wntless (WLS Transporters); Chain length determinant and associated proteins; Sterol-sensing domain (SSD) proteins; Energy-coupling factor (ECF) transporters; Host-defense proteins; Cellulose synthase; Autoinducer exporters; Amino acid secondary transporters; Yellow stripe 1 transporter; Sec, translocase, and insertase proteins; Antiporters; Cysteine proteases; and PIN-FORMED (PIN) proteins. (B) Family groups of β-barrel MPs. β-barrel MPs family includes one report of porins and relatives and one of monomeric/dimeric. Adventitious MPs included a report of β-sheet pore-forming toxins/attack complexes. (C) Total structure weight distribution of all unique reports of membrane proteins identified in this work. Total structure weight comprises the molecular weight of all non-water atoms in the PDB deposited model. The family groups were classified according to the family name provided by the mpstruc database (https://blanco.biomol.uci.edu/mpstruc/ accessed on 14 August 2023). GPCRs: G-protein coupled receptors; SLC: solute carrier; ABC: ATP-binding cassette; PTS: phosphoenolpyruvate-dependent phosphotransferase: MFS: major facilitator superfamily; SSS: solute sodium symporter; APC: Amino Acid/Polyamine/Organocation.