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![[Figure 1]](jc5013fig1mag.jpg)
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Figure 1
Sequence alignment of BT3990, BT3965 and BT3130. Primary-sequence and structural alignments were performed using the PROMALS3D server (Pei et al., 2008  ). Conserved residues are indicated by asterisks above the alignment, α-helices are shown in red and β-strands are shown in blue. Consensus residues are indicated below the alignment: conserved amino acids are in bold uppercase letters, aliphatic residues (I, V, L) are labelled l, aromatic residues (Y, H, W, F) are labelled @, hydrophobic residues (W, F, Y, M, L, I, V, A, C, T, H) are labelled h, alcohol residues (S, T) are labelled o, polar residues (D, E, H, K, N, Q, R, S, T) are labelled p, tiny residues (A, G, C, S) are labelled t, small residues (A, G, C, S, V, N, D, T, P) are labelled s, bulky residues (E, F, I, K, L, M, Q, R, W, Y) are labelled b, positively charged residues (K, R, H) are labelled +, negatively charged resdidues (D, E) are labelled − and charged residues (D, E, K, R, H) are labelled c. Consensus secondary-structure motifs are shown on the lower line: a bold red h indicates α-helix and a bold blue s indicates β-strand. Catalytic acid and base residues are shown in bold on a yellow background. |
![[Figure 1]](jc5013fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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