Crystal structure analysis of cp1 bound BCL2/G101V. Determined by X-ray diffraction at 1.85 Å resolution. Released 15 Nov 2023.
Explore 7YA5 in 3D Show helices and sheets RCSB PDB PDBe
7YA5 contains 10 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 11-25 | 15 | |
| α-helix | 90-107 | 18 | |
| α-helix | 109-116 | 8 | |
| α-helix | 126-138 | 13 | |
| α-helix | 144-163 | 20 | |
| α-helix | 169-180 | 12 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-202 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-9 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator Bcl-2 | A | protein | 166 | Homo sapiens | P10415 (AlphaFold model) |
| cp1 peptide | B | protein | 12 | synthetic construct |
>7YA5_1 Apoptosis regulator Bcl-2 (chains A) MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDDVEENRTEAPEGTESEVVHLTLRQAV DDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVES VNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMR
>7YA5_2 cp1 peptide (chains B) CPARYGWDYECX
| ID | Name | Formula | Copies |
|---|---|---|---|
| JFF | (2R)-3-[2-(aminomethyl)-3-azanyl-1-[4-[2-(2-chloranylethanoylamino)ethylcarbamo… | C19 H26 Cl N5 O6 S | 1 |
Cyclic peptides discriminate BCL-2 and its clinical mutants from BCL-X L by engaging a single-residue discrepancy. Li, F., Liu, J., Liu, C. et al. Nat Commun (2024) 15:1476-1476. DOI 10.1038/s41467-024-45848-1 · PubMed
Other PDB entries of the same protein (UniProt P10415 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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