Human pro-apoptotic protein bid. Determined by solution NMR. Released 2 Feb 2000.
Explore 2BID in 3D Show helices and sheets RCSB PDB PDBe
2BID contains 12 α-helices and 0 β-strands across 1 chain. 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 | 17-29 | 13 | |
| α-helix | 36-42 | 7 | |
| α-helix | 43-45 | 3 | |
| α-helix | 81-100 | 20 | |
| α-helix | 108-116 | 9 | |
| α-helix | 118-120 | 3 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-137 | 12 | |
| α-helix | 147-164 | 18 | |
| α-helix | 169-179 | 11 | |
| α-helix | 180-184 | 5 | |
| α-helix | 185-193 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (BID) | A | protein | 197 | Homo sapiens | P55957 (AlphaFold model) |
>2BID_1 PROTEIN (BID) (chains A) GSMDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQ TDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSR SEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFI NQNLRTYVRSLARNGMD
Solution structure of BID, an intracellular amplifier of apoptotic signaling. Chou, J.J., Li, H., Salvesen, G.S. et al. Cell (1999) 96:615-624. DOI 10.1016/S0092-8674(00)80572-3 · PubMed
Other PDB entries of the same protein (UniProt P55957 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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