Crystal structure of Bcl-xL in complex with BID BH3 domain. Determined by X-ray diffraction at 2.05 Å resolution. Released 10 Jun 2015.
Explore 4QVE in 3D Show helices and sheets RCSB PDB PDBe
4QVE 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 | 5-19 | 15 | |
| α-helix | 86-102 | 17 | |
| α-helix | 109-112 | 4 | |
| α-helix | 119-130 | 12 | |
| α-helix | 137-156 | 20 | |
| α-helix | 161-173 | 13 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 79-96 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bcl-2-like protein 1 | A | protein | 169 | Homo sapiens | Q07817 (AlphaFold model) |
| Peptide from BH3-interacting domain death agonist | B | protein | 34 | Homo sapiens | P55957 (AlphaFold model) |
>4QVE_1 Bcl-2-like protein 1 (chains A) MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEAVKQALREAGDEFELR YRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQ VLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
>4QVE_2 Peptide from BH3-interacting domain death agonist (chains B) SESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGL
Bh3 induced conformational changes in Bcl-Xl revealed by crystal structure and comparative analysis. Rajan, S., Choi, M., Baek, K. et al. Proteins (2015) 83:1262-1272. DOI 10.1002/prot.24816 · 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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