journal menu
![[Figure 3]](ba0010fig3mag.jpg)
|
|
Figure 3
HOMSTRAD database. Structure-based alignment of proteins in the family of cytochrome c. The first four characters of the code of the protein corresponds to the PDB code. Numbers in brackets correspond to residue numbers and residues are shown in single letter code. The alignment has been formatted using JOY (Overington et al., 1990  ). The conserved helices are important to the structural integrity of the proteins; functionally important residues (for example CXXCH, residue number 13 of 1ycc) are conserved. Residues are classified into two categories: those which are in the interior and those which are solvent-exposed (with solvent accessibility (ASA) values more than 7% (Hubbard & Blundell, 1987). In the sequence alignment, the solvent-exposed and solvent-buried residues are shown in lower case and upper case, respectively. Residues which have a positive φ value and a cis-peptide bond in their backbone conformation are shown in italics and with a breve accent on top, respectively. Disulfide-bonded cystine residues are shown by a cedilla symbol. Hydrogen bonding to other side chains, main-chain amides and main-chain carbonyl groups are shown by a tilde (indicated in non-HTML files), in bold and underlined, respectively. Residues in β-strands, α-helices and 3(10)-helices are shown in blue, red and maroon, respectively. |
![[Figure 3]](ba0010fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
