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Figure S9

July 2010

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CC BY 4.0

Authors:

Simeon O Kotchoni

Rutgers, The State University of New Jersey

Vincent Edwards

College of Western Idaho

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Detail structural conformation and conservation analysis of rice ALDH family 12 (ALDH12A1). (A, B, D) The structural description is similar to that of Figure S3 with the exception of superimposition. The secondary structure elements (A) are shown in different colours: α-helix (red), β-sheet (yellow) and coils (green). (C) The space-filled representation of van der Waals surface of the cofactor, and the catalytic opposite positioned amino acids Cys 331 (green) and Glu 435 (red) are shown. (8.15 MB TIF)

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Modeling-Dependent Protein Characterization of the Rice Aldehyde Dehydrogenase (ALDH) Superfamily Reveals Distinct Functional and Structural Features

Article

July 2010

Simeon O Kotchoni · Jose C Jimenez-Lopez · Dongying Gao · Vincent Edwards · Manfredo Seufferheld

Data

Full-text available

Figure S13

July 2010

Detail structural conformation and conservation analysis of rice ALDH family 22 (ALDH22A1). (A, B, D) The structural description is similar to that of Figure S3 with the exception of superimposition. The secondary structure elements (A) are shown in different colours: α-helix (red), α-sheet (yellow) and coils (green). (C) The space-filled representation of van der Waals surface of the cofactor, ... [Show full abstract] and the catalytic opposite positioned amino acids Cys 332 (green) and Glu 433 (red) are shown. (8.99 MB TIF)

Data

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Figure S8

July 2010

Detail structural conformation and conservation analysis of rice ALDH family 11 (ALDH11A3). (A, B, D) The structural description is similar to that of Figure S3 with the exception of superimposition. The secondary structure elements (A) are shown in different colours: α-helix (red), β-sheet (yellow) and coils (green). (C) The space-filled representation of van der Waals surface of the cofactor, ... [Show full abstract] and the catalytic opposite positioned amino acids Cys 301 (green) and Glu 394 (red) are shown. (9.04 MB TIF)

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Figure S6

July 2010

Detail structural conformation and conservation analysis of rice ALDH family 7 (ALDH7B6). (A, B, D) The structural description is similar to that of Figure S3 with the exception of superimposition. The secondary structure elements (A) are shown in different colours: α-helix (red), β-sheet (yellow) and coils (green). (C) The space-filled representation of van der Waals surface of the cofactor, and ... [Show full abstract] the catalytic opposite positioned amino acids Cys 301 (green) and Glu 397 (red) are shown. (8.42 MB TIF)

Data

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Figure S5

July 2010

Detail structural conformation and conservation analysis of rice ALDH family 6 (ALDH6B1). (A, B, D) Detail description similar to that of Figure S3 with the exception of superimposition. The secondary structure elements are depicted in different colours: α-helix (red), β-sheet (yellow) and coils (green). (C) Space-filled representation of van der Waals surface of the cofactor, and the catalytic ... [Show full abstract] opposite positioned amino acids Cys 318 (green) and Glu 418 (red) are here shown. (8.55 MB TIF)

Last Updated: 27 May 2025