Structural basis of autoactivation of P38 alpha induced by TAB1 (tetragonal crystal form)

Structure

x-ray diffraction · 6 distinct chains · 38% helix, 15% strand (DSSP).

Ligands and binding sites

• SB4 · 4-(4-fluorophenyl)-1-(4-piperidinyl)-5-(2-amino-4-pyrimidinyl)-imidazole · ligand · 4 copies · chains A, B, L, C, K, D
• EDO · 1,2-ethanediol · additive · 15 copies · chains A, C, B, D, L
• TLA · L(+)-tartaric acid · additive · 2 copies · chains A, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Interfaces

13 interfaces between chains.

• B–D · 1442 Ų buried · 27 hydrogen bonds · protein-protein
• A–C · 1416 Ų buried · 23 hydrogen bonds · protein-protein
• C–K · 1222 Ų buried · 15 hydrogen bonds · protein-protein
• B–L · 1209 Ų buried · 14 hydrogen bonds · protein-protein
• D–N · 1083 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

• 4LOP · Structural basis of autoactivation of p38 alpha induced by TAB1 (Tetragonal crystal form) · the same entry in another collection · chain N against N, TM-score 1.00
• P47811 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 14 (P47811) · a predicted model of the same protein · chain C against A, TM-score 0.97
• Q8CF89 · AlphaFold monomer V2.0 prediction for TGF-beta-activated kinase 1 and MAP3K7-binding… · a predicted model of the same protein · chain M against A, TM-score 0.24

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 P47811
• Every structure of UniProt Q8CF89
• Elsewhere: RCSB PDB 4LOP · PDBe 4LOP · UniProt P47811 · UniProt Q8CF89