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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites

Fig. 1

Homologous modeling of CTendo45 using the Thielavia terrestris β-1,4-endoglucanase TtCel45A (PDB: 5GLY) as a template. a The solvent accessible surface. Cellotriose and cellotetraose molecules, bound in the substrate-binding cleft, are shown in cyan. The branched N-glycan attached to the residue Asn88 in CTendo45 is represented as a white and red stick. The V–VI loop is noted in purple. Catalytic residues and the additional histidine residues are noted in orange and yellow, respectively. The intrinsic histidine residue was noted in red. b The 3D superposition between CTendo45 (marine) and TtCel45A (wheat). The spatial positions of valuable residues used in this study are marked by colored sticks. A front view of substrate-binding cleft. c Rotating the configuration 90° anti-clockwise. d Rotating 90° clockwise. All of the structural diagrams were drawn using PyMOL software

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