3SL9: Beta catenin
X-ray structure of Beta catenin in complex with Bcl9. Determined by X-ray diffraction at 2.2 Å resolution. Released 29 Feb 2012.
- Method
- X-ray diffraction
- Resolution
- 2.2 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 5,813
- Mol. weight
- 99.55 kDa
- Released
- 29 Feb 2012
Explore 3SL9 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3SL9 contains 50 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 | 144-160 | 17 | |
| α-helix | 165-179 | 15 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 208-221 | 14 | |
| α-helix | 225-233 | 9 | |
| α-helix | 236-243 | 8 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-285 | 8 | |
| α-helix | 291-304 | 14 | |
Chain B: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 142-160 | 19 | |
| α-helix | 165-179 | 15 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 208-221 | 14 | |
| α-helix | 225-233 | 9 | |
| α-helix | 236-243 | 8 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-288 | 11 | |
| α-helix | 291-293 | 3 | |
| α-helix | 294-304 | 11 | |
Chains C, D and F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 353-373 | 21 | |
Chain E: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 142-160 | 19 | |
| α-helix | 165-178 | 14 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 208-221 | 14 | |
| α-helix | 225-233 | 9 | |
| α-helix | 236-243 | 8 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-288 | 11 | |
| α-helix | 291-293 | 3 | |
| α-helix | 294-304 | 11 | |
Chain G: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 154-160 | 7 | |
| α-helix | 165-178 | 14 | |
| α-helix | 182-189 | 8 | |
| α-helix | 192-204 | 13 | |
| α-helix | 208-222 | 15 | |
| α-helix | 225-233 | 9 | |
| α-helix | 236-243 | 8 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-285 | 8 | |
| α-helix | 291-304 | 14 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 353-367 | 15 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Catenin beta-1 | A, B, E, G | protein | 167 | Homo sapiens | P35222 (AlphaFold model) |
| B-cell CLL/lymphoma 9 protein | C, D, F, H | protein | 55 | Homo sapiens | O00512 (AlphaFold model) |
Sequence of entity 1 (A, B, E, G), FASTA
>3SL9_1 Catenin beta-1 (chains A, B, E, G)
GSNYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAI
VRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITT
LHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILA
Sequence of entity 2 (C, D, F, H), FASTA
>3SL9_2 B-cell CLL/lymphoma 9 protein (chains C, D, F, H)
MALGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTGAQSGGPQQNPGVLD
Primary citation
An intrinsically labile alpha-helix abutting the BCL9-binding site of beta-catenin is required for its inhibition by carnosic acid. de la Roche, M., Rutherford, T.J., Gupta, D. et al. Nat Commun (2012) 3:680-680. DOI 10.1038/ncomms1680 · PubMed
Other PDB entries of the same protein (UniProt P35222 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3FQN 1.65 Å, Phosphorylation of self-peptides alters Human Leukocyte Antigen Class I-restricted…
- 3FQR 1.7 Å, Phosphorylation of self-peptides alters Human Leukocyte Antigen Class I-restricted…
- 7AFW 1.81 Å, Beta-Catenin in complex with compound 6
- 1JDH 1.9 Å, Crystal structure of beta-catenin and htcf-4
- 9I8K 2.0 Å, Beta-catenin armadillo (150-663)
- 9I8X 2.0 Å, Beta-catenin armadillo with cyclic peptide and Compound 2
- 8RU3 2.0 Å, Crystal structure of beta-catenin in complex with alpha-helical peptide inhibitor
- 6M90 2.05 Å, Monophosphorylated pSer33 b-Catenin peptide, b-TrCP/Skp1, NRX-2776 ternary complex
- 29KL 2.09 Å, Crystal structure of Human Catenin Beta-1 in complex with cyclic beta sheet peptide…
- 1G3J 2.1 Å, Crystal structure of the XTCF3-cbd/beta-catenin armadillo repeat complex
- 1T08 2.1 Å, Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3
- 3DIW 2.1 Å, c-terminal beta-catenin bound TIP-1 structure
Browse structure collections
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