Bag domain of BAG1 cochaperone. Determined by solution NMR. Released 6 Sept 2001.
Explore 1I6Z in 3D Show helices and sheets RCSB PDB PDBe
1I6Z contains 3 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 98-132 | 35 | |
| α-helix | 138-167 | 30 | |
| α-helix | 176-210 | 35 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bag-family molecular chaperone regulator-1 | A | protein | 135 | Mus musculus | Q60739 (AlphaFold model) |
>1I6Z_1 BAG-FAMILY MOLECULAR CHAPERONE REGULATOR-1 (chains A) GSPEFMLIGEKSNPEEEVELKKLKDLEVSAEKIANHLQELNKELSGIQQGFLAKELQAEA LCKLDRKVKATIEQFMKILEEIDTMVLPEQFKDSRLKRKNLVKKVQVFLAECDTVEQYIC QETERLQSTNLALAE
Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Briknarova, K., Takayama, S., Brive, L. et al. Nat Struct Biol (2001) 8:349-352. DOI 10.1038/86236 · PubMed
Other PDB entries of the same protein (UniProt Q60739 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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