› 2eva

X-ray diffraction
2Å resolution

Structural Basis for the Interaction of TAK1 Kinase with its Activating Protein TAB1

Released:
DOI: 10.2210/pdb2eva/pdb
PDB entry 2eva coloured by chain, front view.
PDB entry 2eva coloured by chain, side view.
PDB entry 2eva coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the interaction of TAK1 kinase with its activating protein TAB1.
Brown K, Vial SC, Dedi N, Long JM, Dunster NJ, Cheetham GM
J Mol Biol 354 1013-20 (2005)
PMID: 16289117

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase kinase kinase 7 Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 34.78 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O43318 (Residues: 31-305; Coverage: 45%)
Gene names: MAP3K7, TAK1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADN 1 x ADN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: I222
Unit cell:
a: 58.4Å b: 144.3Å c: 134.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.258 0.212 0.231
Expression system: Spodoptera frugiperda

Quick links

Citations

13 review citations

Molecular basis of NF-κB signaling.
Napetschnig et al. (2013)
12 more

24 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
23 more