2GL7: Beta-catenin/BCL9/Tcf4 complex
Crystal Structure of a beta-catenin/BCL9/Tcf4 complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 31 Oct 2006.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 8,429
- Mol. weight
- 142.32 kDa
- Released
- 31 Oct 2006
Explore 2GL7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2GL7 contains 82 α-helices and 4 β-strands across 6 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: 37 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 143-160 | 18 | |
| α-helix | 165-180 | 16 | |
| 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 | 278-284 | 7 | |
| α-helix | 285-287 | 3 | |
| α-helix | 291-305 | 15 | |
| α-helix | 309-317 | 9 | |
| α-helix | 320-328 | 9 | |
| α-helix | 334-347 | 14 | |
| α-helix | 353-359 | 7 | |
| α-helix | 362-367 | 6 | |
| α-helix | 375-388 | 14 | |
| α-helix | 389-391 | 3 | |
| α-helix | 399-408 | 10 | |
| α-helix | 414-428 | 15 | |
| α-helix | 432-440 | 9 | |
| α-helix | 443-454 | 12 | |
| α-helix | 458-471 | 14 | |
| α-helix | 478-487 | 10 | |
| α-helix | 490-497 | 8 | |
| α-helix | 504-517 | 14 | |
| α-helix | 521-529 | 9 | |
| α-helix | 532-548 | 17 | |
| β-strand | 561 | 1 | 1 |
| β-strand | 564 | 1 | 1 |
| α-helix | 566-580 | 15 | |
| α-helix | 584-592 | 9 | |
| α-helix | 596-601 | 6 | |
| α-helix | 602-604 | 3 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-633 | 9 | |
| α-helix | 637-642 | 6 | |
| α-helix | 649-660 | 12 | |
Chain B: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-16 | 3 | |
| α-helix | 39-48 | 10 | |
Chain C: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 353-373 | 21 | |
Chain D: 39 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 149-160 | 12 | |
| 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 | 236-242 | 7 | |
| α-helix | 243-245 | 3 | |
| α-helix | 249-265 | 17 | |
| α-helix | 269-275 | 7 | |
| α-helix | 278-284 | 7 | |
| α-helix | 285-287 | 3 | |
| α-helix | 291-305 | 15 | |
| α-helix | 309-317 | 9 | |
| α-helix | 320-330 | 11 | |
| α-helix | 334-347 | 14 | |
| α-helix | 353-359 | 7 | |
| α-helix | 362-367 | 6 | |
| α-helix | 375-388 | 14 | |
| α-helix | 389-391 | 3 | |
| α-helix | 399-408 | 10 | |
| α-helix | 414-428 | 15 | |
| α-helix | 432-440 | 9 | |
| α-helix | 443-454 | 12 | |
| α-helix | 458-471 | 14 | |
| α-helix | 478-487 | 10 | |
| α-helix | 491-496 | 6 | |
| α-helix | 504-517 | 14 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-529 | 6 | |
| α-helix | 532-548 | 17 | |
| β-strand | 561 | 1 | 2 |
| β-strand | 564 | 1 | 2 |
| α-helix | 566-580 | 15 | |
| α-helix | 584-591 | 8 | |
| α-helix | 596-601 | 6 | |
| α-helix | 602-604 | 3 | |
| α-helix | 608-621 | 14 | |
| α-helix | 625-633 | 9 | |
| α-helix | 637-643 | 7 | |
| α-helix | 649-661 | 13 | |
Chain E: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-16 | 3 | |
| α-helix | 42-49 | 8 | |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 356-370 | 15 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Beta-catenin | A, D | protein | 550 | Homo sapiens | P35222 (AlphaFold model) |
| Transcription factor 7-like 2 | B, E | protein | 53 | Homo sapiens | Q9NQB0 (AlphaFold model) |
| B-cell lymphoma 9 protein | C, F | protein | 46 | Homo sapiens | O00512 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>2GL7_1 Beta-catenin (chains A, D)
SNLINEQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVS
AIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAI
TTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIIL
ASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQR
LVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKM
MVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVK
LLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGT
QQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAG
VLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSV
ELTSSLFRTE
Sequence of entity 2 (B, E), FASTA
>2GL7_2 Transcription factor 7-like 2 (chains B, E)
MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESE
Sequence of entity 3 (C, F), FASTA
>2GL7_3 B-cell lymphoma 9 protein (chains C, F)
NPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTGAQSGGPQQNP
Primary citation
Crystal Structure of a beta-Catenin/BCL9/Tcf4 Complex. Sampietro, J., Dahlberg, C.L., Cho, U.S. et al. Mol Cell (2006) 24:293-300. DOI 10.1016/j.molcel.2006.09.001 · 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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