Fig. 5 | Scientific Reports

Fig. 5

From: In silico characterization, structural modeling, and molecular docking of GabP in citrus and its potential role in GABA uptake

Fig. 5

The predicted topology of putative GABA permeases (CsgabP, aka amino-acid permease [BAT1]) from Citrus sinensis. (A and E) Membrane prediction and surface topology of CsgabP-1 (XP_006468761.1), and CsgabP-2 (XP_006468762.1), respectively. (B and G) Membrane prediction and cartoon organization of CsgabP-1 and CsgabP-2, respectively. Bio-units of transmembrane proteins are identified in the SMTL solely based on structural information. The membrane annotation is transferred to a model if at least 80% of all biounit-transmembrane residues are aligned with the target sequence(s). Protein chains are colored according to their hydrophobicity. Low hydrophobic residues are colored blue, whereas most hydrophobic residues are colored red (see the scale at the right bottom corner of the graph). (C and F) Schematic representation of Phyre2-based predicted topology of CsgabP-1, CsgabP-2, and CsgabP-3, respectively. Numbers inside the transmembrane (TM) domains (yellow rectangle) denote AA residues. (D and H) TMHMM posterior probabilities.

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