- Deposition Date: 2004/11/30
- Description: 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33).
- Solution Method: X-RAY (MR)
- Start: 1 End: 290 Sequence Type: Complete
- Fold Function: Disulfide bond chaperone of the HSP33 family; Pfam domain PF01430; COG domain COG1281.
- Fold Summary: Consists of two domains. The first domain, already solved in known HSP33 structures, has beta/alpha/beta architecture with one helix buried between beta strands. The second, smaller domain is a new fold of zinc finger from zinc ribbon foldgroup, consisting of two short helices followed by two-strand beta sheet and the third short helix. Two other structures of this fold have been solved in 2004.
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