Homodimer of BACH1 BTB domain in complex with 2-Methyl-2,4-pentanediol. Determined by X-ray diffraction at 1.47 Å resolution. Released 11 Dec 2024.
Explore 9GRA in 3D Show helices and sheets RCSB PDB PDBe
9GRA contains 13 α-helices and 10 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 9-12 | 4 | 1 |
| α-helix | 16-30 | 15 | |
| β-strand | 36-40 | 5 | 2 |
| β-strand | 43-47 | 5 | 2 |
| α-helix | 49-55 | 7 | |
| α-helix | 57-63 | 7 | |
| β-strand | 71-74 | 4 | 2 |
| α-helix | 81-93 | 13 | |
| β-strand | 95-99 | 5 | 3 |
| α-helix | 103-113 | 11 | |
| α-helix | 120-127 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 3 |
| α-helix | 16-30 | 15 | |
| β-strand | 36-40 | 5 | 4 |
| β-strand | 43-47 | 5 | 4 |
| α-helix | 49-55 | 7 | |
| α-helix | 57-63 | 7 | |
| β-strand | 71-74 | 4 | 4 |
| α-helix | 75-76 | 2 | |
| α-helix | 81-93 | 13 | |
| β-strand | 95-98 | 4 | 1 |
| α-helix | 103-113 | 11 | |
| α-helix | 119-123 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription regulator protein BACH1 | A, B | protein | 124 | Homo sapiens | O14867 (AlphaFold model) |
>9GRA_1 Transcription regulator protein BACH1 (chains A, B) SMSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIV GQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQ FLKF
| ID | Name | Formula | Copies |
|---|---|---|---|
| MRD | (4R)-2-methylpentane-2,4-diol | C6 H14 O2 | 1 |
Dual BACH1 regulation by complementary SCF-type E3 ligases. Goretzki, B., Khoshouei, M., Schroder, M. et al. Cell (2024) 187:7585-7602.e25. DOI 10.1016/j.cell.2024.11.006 · PubMed
Other PDB entries of the same protein (UniProt O14867 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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