Complex of bcl-xl with peptide from bad. Determined by solution NMR. Released 7 Feb 2001.
Explore 1G5J in 3D Show helices and sheets RCSB PDB PDBe
1G5J contains 13 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 | 3-5 | 3 | |
| α-helix | 6-24 | 19 | |
| α-helix | 28-30 | 3 | |
| α-helix | 46-104 | 19 | |
| α-helix | 106-109 | 4 | |
| α-helix | 123-135 | 13 | |
| α-helix | 140-160 | 21 | |
| α-helix | 165-176 | 12 | |
| α-helix | 177-181 | 5 | |
| α-helix | 184-189 | 6 | |
| α-helix | 191-199 | 9 | |
| α-helix | 201-211 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 304-319 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apoptosis regulator bcl-X | A | protein | 175 | Homo sapiens | Q07817 (AlphaFold model) |
| Bad protein | B | protein | 25 | Q92934 (AlphaFold model) |
>1G5J_1 APOPTOSIS REGULATOR BCL-X (chains A) MSMAMSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEAVKQALREAGDE FELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVD KEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERLE
>1G5J_2 BAD PROTEIN (chains B) NLWAAQRYGRELRRMSDEFVDSFKK
Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. Petros, A.M., Nettesheim, D.G., Wang, Y. et al. Protein Sci (2000) 9:2528-2534. DOI 10.1017/S096183680000331X · PubMed
Other PDB entries of the same protein (UniProt Q07817 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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