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Fig. 3 | BMC Research Notes

Fig. 3

From: Functional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms

Fig. 3

Homology modeling of OsttaSSIIIs SBDs. a Structural model of Rattus norvegicus AMPK β-subunit GBD (RatnoAMPK-β, PDB code: 1Z0N), Bacillus halodurans amylase CBM25 (BachaCBM25, PDB code: 2C3V) and Paenibacillus polymyxa amylase CBM25 (PaepoCBM25, PDB code: 2LAA); binding residues are shown. b Proposed models for OsttaSSIII-A D1, OsttaSSIII-A D2, OsttaSSIII-B D1, OsttaSSIII-B D2 and OsttaSSIII-B D3; putative binding residues are shown. Superimposition of OsttaSSIII-A D1, OsttaSSIII-A D2, OsttaSSIII-B D1, OsttaSSIII-B D2 and OsttaSSIII-B D3 binding residues (red) and 1Z0N or 2C3V (cyan) binding residues, is shown next to each model

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