4TUH: Bcl-xL
Bcl-xL in complex with inhibitor (Compound 10). Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Oct 2014.
- Method
- X-ray diffraction
- Resolution
- 1.8 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 10,587
- Mol. weight
- 149.78 kDa
- Ligands
- 38H
- Released
- 15 Oct 2014
Explore 4TUH in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4TUH contains 85 α-helices and 0 β-strands across 8 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.
Chain A: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-19 | 20 | |
| α-helix | 26-96 | 15 | |
| α-helix | 97-101 | 5 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-112 | 5 | |
| α-helix | 120-130 | 11 | |
| 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 | |
Chain B: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-19 | 18 | |
| α-helix | 84-96 | 13 | |
| α-helix | 97-101 | 5 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-112 | 5 | |
| α-helix | 120-130 | 11 | |
| 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 | |
Chain C: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-19 | 19 | |
| α-helix | 26-100 | 19 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 120-130 | 11 | |
| α-helix | 137-156 | 20 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
Chains D and G: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 26-100 | 19 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-112 | 5 | |
| α-helix | 120-130 | 11 | |
| α-helix | 137-156 | 20 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
Chain E: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-19 | 18 | |
| α-helix | 84-96 | 13 | |
| α-helix | 97-101 | 5 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 120-127 | 8 | |
| α-helix | 137-156 | 20 | |
| α-helix | 160-162 | 3 | |
| α-helix | 163-173 | 11 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
Chain F: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-19 | 20 | |
| α-helix | 26-100 | 19 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-112 | 5 | |
| α-helix | 120-130 | 11 | |
| 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 | |
Chain H: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-19 | 20 | |
| α-helix | 26-100 | 19 | |
| α-helix | 102-104 | 3 | |
| α-helix | 108-112 | 5 | |
| α-helix | 120-128 | 9 | |
| α-helix | 129-131 | 3 | |
| α-helix | 137-156 | 20 | |
| α-helix | 162-173 | 12 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-184 | 6 | |
| α-helix | 187-195 | 9 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Bcl-2-like protein 1 | A, B, C, D, E, F, G, H | protein | 158 | Homo sapiens | Q07817 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>4TUH_1 Bcl-2-like protein 1 (chains A, B, C, D, E, F, G, H)
GPLGSMSQSNRELVVDFLSYKLSQKGYSWSQMAAVKQALREAGDEFELRYRRAFSDLTSQ
LHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMA
TYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQER
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 38H | 2-[8-(1,3-benzothiazol-2-ylcarbamoyl)-3,4-dihydroisoquinolin-2(1H)-yl]-5-{3-[4-… | C35 H28 N8 O4 S2 | 8 |
Water and common crystallization additives (ACT, EDO) are not listed.
Primary citation
Structure-Guided Rescaffolding of Selective Antagonists of BCL-XL. Koehler, M.F., Bergeron, P., Choo, E.F. et al. ACS Med Chem Lett (2014) 5:662-667. DOI 10.1021/ml500030p · PubMed
Other PDB entries of the same protein (UniProt Q07817 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7JGW 1.3 Å, Crystal structure of BCL-XL in complex with COMPOUND 1620116, CRYSTAL FORM 1
- 3SP7 1.4 Å, Crystal Structure of Bcl-xL bound to BM903
- 7YAA 1.4 Å, Crystal structure analysis of cp3 bound BCLxl
- 7LH7 1.41 Å, Crystal structure of BCL-XL in complex with a benzothiazole-based inhibitor
- 9IGG 1.5 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
- 4QVF 1.53 Å, Crystal structure of Bcl-xL in complex with BIM BH3 domain
- 4A1U 1.54 Å, Crystal structure of alpha-beta-foldamer 2c in complex with Bcl-xL
- 6VWC 1.6 Å, Crystal structure of Bcl-xL in complex with tetrahydroisoquinoline-pyridine based…
- 6O0K 1.62 Å, crystal structure of BCL-2 with venetoclax
- 3SPF 1.7 Å, Crystal Structure of Bcl-xL bound to BM501
- 9I9E 1.7 Å, Structure of human Bcl-xL in complex with small molecule inhibitor
- 9O14 1.73 Å, Crystal Structure of BCL-2 in complex with a stapled BAD BH3 peptide BAD SAHB 4.2
Browse structure collections
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