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Structural basis for the interaction of TAK1 kinase with its activating protein TAB1
Analyse Structural basis for the interaction of TAK1 kinase with its activating protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EVA
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43318
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 295 | — | O43318 |
Compared structures
- 2EVA · Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1 · 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
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
- Elsewhere: RCSB PDB 2EVA · PDBe 2EVA · UniProt O43318
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