Crystal structure of human TAK1 kinase domain fused with TAB1. Determined by X-ray diffraction at 2.05 Å resolution. Released 20 Sept 2023.
Explore 8GW3 in 3D Show helices and sheets RCSB PDB PDBe
8GW3 contains 80 α-helices and 56 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 29-30 | 2 | 1 |
| α-helix | 33-35 | 3 | |
| β-strand | 36-40 | 5 | 1 |
| β-strand | 50-55 | 6 | 1 |
| β-strand | 58-64 | 7 | 1 |
| α-helix | 68-76 | 9 | |
| α-helix | 78-82 | 5 | |
| β-strand | 89 | 1 | 2 |
| β-strand | 92-97 | 6 | 1 |
| β-strand | 100-105 | 6 | 1 |
| β-strand | 110-111 | 2 | 2 |
| α-helix | 112-117 | 6 | |
| β-strand | 123 | 1 | 3 |
| α-helix | 127-146 | 20 | |
| α-helix | 151-153 | 3 | |
| α-helix | 159-161 | 3 | |
| β-strand | 162-165 | 4 | 2 |
| β-strand | 170-173 | 4 | 2 |
| α-helix | 182-185 | 4 | |
| α-helix | 193-195 | 3 | |
| α-helix | 198-203 | 6 | |
| α-helix | 208-224 | 17 | |
| α-helix | 237-244 | 8 | |
| α-helix | 249-251 | 3 | |
| β-strand | 252 | 1 | 4 |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-287 | 11 | |
| α-helix | 288-290 | 3 | |
| α-helix | 297-298 | 2 | |
| β-strand | 301 | 1 | 3 |
| β-strand | 478 | 1 | 4 |
| α-helix | 485-495 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-30 | 2 | 5 |
| α-helix | 33-35 | 3 | |
| β-strand | 36-40 | 5 | 5 |
| β-strand | 50-55 | 6 | 5 |
| β-strand | 58-64 | 7 | 5 |
| α-helix | 68-76 | 9 | |
| α-helix | 78-82 | 5 | |
| β-strand | 89 | 1 | 6 |
| β-strand | 92-97 | 6 | 5 |
| β-strand | 100-105 | 6 | 5 |
| β-strand | 110-111 | 2 | 6 |
| α-helix | 112-117 | 6 | |
| β-strand | 123 | 1 | 7 |
| α-helix | 127-146 | 20 | |
| α-helix | 151-153 | 3 | |
| α-helix | 159-161 | 3 | |
| β-strand | 162-165 | 4 | 6 |
| β-strand | 170-173 | 4 | 6 |
| α-helix | 182-187 | 6 | |
| α-helix | 193-195 | 3 | |
| α-helix | 198-201 | 4 | |
| α-helix | 204-206 | 3 | |
| α-helix | 208-224 | 17 | |
| α-helix | 236-244 | 9 | |
| α-helix | 249-251 | 3 | |
| β-strand | 252 | 1 | 8 |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-287 | 11 | |
| α-helix | 288-290 | 3 | |
| α-helix | 297-298 | 2 | |
| β-strand | 301 | 1 | 7 |
| β-strand | 478 | 1 | 8 |
| α-helix | 485-495 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-31 | 3 | 9 |
| α-helix | 33-35 | 3 | |
| β-strand | 36-40 | 5 | 9 |
| β-strand | 50-55 | 6 | 9 |
| β-strand | 58-64 | 7 | 9 |
| α-helix | 68-81 | 14 | |
| β-strand | 89 | 1 | 10 |
| β-strand | 92-97 | 6 | 9 |
| β-strand | 100-105 | 6 | 9 |
| β-strand | 110-111 | 2 | 10 |
| α-helix | 112-117 | 6 | |
| β-strand | 123 | 1 | 11 |
| α-helix | 127-146 | 20 | |
| α-helix | 151-153 | 3 | |
| α-helix | 159-161 | 3 | |
| β-strand | 162-165 | 4 | 10 |
| β-strand | 170-173 | 4 | 10 |
| α-helix | 193-195 | 3 | |
| α-helix | 198-202 | 5 | |
| α-helix | 204-206 | 3 | |
| α-helix | 208-224 | 17 | |
| α-helix | 236-244 | 9 | |
| α-helix | 249-251 | 3 | |
| β-strand | 252 | 1 | 12 |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-287 | 11 | |
| α-helix | 288-290 | 3 | |
| α-helix | 297-298 | 2 | |
| β-strand | 301 | 1 | 11 |
| β-strand | 478 | 1 | 12 |
| α-helix | 485-495 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-30 | 2 | 13 |
| α-helix | 33-35 | 3 | |
| β-strand | 36-40 | 5 | 13 |
| β-strand | 50-55 | 6 | 13 |
| β-strand | 58-64 | 7 | 13 |
| α-helix | 68-83 | 16 | |
| β-strand | 89 | 1 | 14 |
| β-strand | 92-97 | 6 | 13 |
| β-strand | 100-105 | 6 | 13 |
| β-strand | 110-111 | 2 | 14 |
| α-helix | 112-117 | 6 | |
| β-strand | 123 | 1 | 15 |
| α-helix | 127-146 | 20 | |
| α-helix | 151-153 | 3 | |
| α-helix | 159-161 | 3 | |
| β-strand | 162-165 | 4 | 14 |
| β-strand | 170-173 | 4 | 14 |
| α-helix | 185-187 | 3 | |
| α-helix | 193-195 | 3 | |
| α-helix | 198-202 | 5 | |
| α-helix | 204-206 | 3 | |
| α-helix | 208-224 | 17 | |
| α-helix | 236-244 | 9 | |
| α-helix | 249-251 | 3 | |
| β-strand | 252 | 1 | 16 |
| α-helix | 257-266 | 10 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-276 | 2 | |
| α-helix | 277-287 | 11 | |
| α-helix | 288-290 | 3 | |
| α-helix | 297-298 | 2 | |
| β-strand | 301 | 1 | 15 |
| β-strand | 478 | 1 | 16 |
| α-helix | 485-494 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase kinase kinase 7, TGF-beta-activated kinase 1 and MAP3K7-binding… | A, B, C, D | protein | 326 | Homo sapiens | O43318 (AlphaFold model), Q15750 (AlphaFold model) |
>8GW3_1 Mitogen-activated protein kinase kinase kinase 7, TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 (chains A, B, C, D) AGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAF IVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWC LQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAA WMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKN LPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQHSLPPGEDGRV EPYVDFAEFYRLWSVDHGEQSVVTAP
Crystal structure of human TAK1 kinase domain fused with TAB1. Liu, J., Sun, W., Gao, J. To be published.
Other PDB entries of the same protein (UniProt O43318 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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