Crystal Structure of TEL SAM Polymer. Determined by X-ray diffraction at 1.45 Å resolution. Released 3 Jul 2002.
Explore 1JI7 in 3D Show helices and sheets RCSB PDB PDBe
1JI7 contains 22 α-helices and 0 β-strands across 3 chains. 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 | 20-22 | 3 | |
| α-helix | 26-28 | 3 | |
| α-helix | 31-44 | 14 | |
| α-helix | 47 | 1 | |
| α-helix | 49 | 1 | |
| α-helix | 59-62 | 4 | |
| α-helix | 67-73 | 7 | |
| α-helix | 78-90 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-22 | 3 | |
| α-helix | 26-28 | 3 | |
| α-helix | 31-45 | 15 | |
| α-helix | 47-49 | 3 | |
| α-helix | 52-55 | 4 | |
| α-helix | 59-62 | 4 | |
| α-helix | 67-73 | 7 | |
| α-helix | 78-90 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-22 | 3 | |
| α-helix | 26-28 | 3 | |
| α-helix | 31-44 | 14 | |
| α-helix | 59-62 | 4 | |
| α-helix | 67-73 | 7 | |
| α-helix | 78-97 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ets-related protein TEL1 | A, B, C | protein | 89 | Homo sapiens | P41212 (AlphaFold model) |
>1JI7_1 ETS-RELATED PROTEIN TEL1 (chains A, B, C) SIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRS PHSGDELYELLQHILKQRDHHHHHHHRHD
Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression. Kim, C.A., Phillips, M.L., Kim, W. et al. EMBO J (2001) 20:4173-4182. DOI 10.1093/emboj/20.15.4173 · PubMed
Other PDB entries of the same protein (UniProt P41212 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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