Alpha + Beta Folds |
Alpha/Beta Doubly-Wound Folds
The doubly wound alpha/beta topology was described on the
previous page. Some variations of the
classic doubly wound fold are illustrated here. In the topology diagrams
below, the parts of the chain linking the beta-strands are red, and are thick
when they include an alpha-helix. In the RasMol scripts, non-alpha-helical
linking regions are shown in pink. Some of the scripts highlight in blue
where the fold begins.
flavodoxin, 1flv (127Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
subtilisin, 1sbt (172Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
arabinose-binding protein, domain 1, 5abp (217Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
glyceraldehyde phosphate dehydrogenase, 3gpd (443Kb) [Bbk|BNL|ExP|Waw|Hal] ... SCRIPT
dihydrofolate reductase, 3dfr (157Kb) [Bbk|BNL|ExP|Waw|Hal]
adenylate kinase, 3adk (135Kb) [Bbk|BNL|ExP|Waw|Hal]
rhodanese domain 1, 1rhd (202Kb) [Bbk|BNL|ExP|Waw|Hal]
glutathione reductase, 1gra (366Kb) [Bbk|BNL|ExP|Waw|Hal]
carboxypeptidase, 2ctb (Kb) [Bbk|BNL|ExP|Waw|Hal] This fold varies considerably from a classic doubly-wound variation in order to achieve the arrangement of sheet (mixed parallel and antiparallel in this case).
Alpha + Beta Folds |
Last updated 7th April '97