Research workbench
Crystal structure of human TAK1/TAB1 fusion protein in complex with ligand 11C
Analyse Crystal structure of human TAK1/TAB1 fusion protein in complex with ligand 11C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JGA
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TAK1 kinase - TAB1 chimera fusion protein
- EC
- 2.7.11.25
- UniProt
- O43318, Q15750
- Ligands
- 6KC
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TAK1 kinase - TAB1 chimera fusion protein (EC 2.7.11.25) | protein | 296 | 39% helix, 18% strand | O43318, Q15750 |
Ligands and binding sites
- 6KC · N-[5-(4-methylpiperazine-1-carbonyl)[1,1'-biphenyl]-2-yl]-4-oxo-3,4-dihydrothieno[3,2-d]pyrimidine-7-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.58 | 0.82 | 22 | 6KC |
| 2 | 58 | 0.31 | 0.76 | 15 | empty |
| 3 | 55 | 0.29 | 0.75 | 14 | empty |
| 4 | 51 | 0.28 | 0.75 | 17 | empty |
Compared structures
- 5JGA · Crystal structure of human TAK1/TAB1 fusion protein in complex with ligand 11c · the same entry in another collection · chain A against A, TM-score 1.00
- O43318 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase kinase kinase 7… · a predicted model of the same protein · chain A against A, TM-score 0.93
- Q15750 · AlphaFold monomer V2.0 prediction for TGF-beta-activated kinase 1 and MAP3K7-binding… · a predicted model of the same protein · chain A against A, TM-score 0.29
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O43318
- Every structure of UniProt Q15750
- Elsewhere: RCSB PDB 5JGA · PDBe 5JGA · UniProt O43318 · UniProt Q15750
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