The crystal structure of NAP1 in complex with TBK1

Structure

x-ray diffraction · 3 distinct chains · 82% helix, 5% strand (DSSP).

Ligands and binding sites

• GOL · Glycerol · additive · 5 copies · chains A, C, D

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

Interfaces

6 interfaces between chains.

• A–D · 932 Ų buried · 9 hydrogen bonds · protein-protein
• A–B · 928 Ų buried · 5 hydrogen bonds · protein-protein
• C–D · 911 Ų buried · 2 hydrogen bonds · protein-protein
• C–B · 850 Ų buried · 5 hydrogen bonds · protein-protein
• B–D · 784 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

• 5EP6 · The crystal structure of NAP1 in complex with TBK1 · the same entry in another collection · chain A against A, TM-score 1.00
• Q9H6S1 · AlphaFold monomer V2.0 prediction for 5-azacytidine-induced protein 2 (Q9H6S1) · a predicted model of the same protein · chain C against A, TM-score 0.88
• Q9UHD2 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase TBK1 (Q9UHD2) · a predicted model of the same protein · chain B against A, TM-score 0.78

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 Q9H6S1
• Every structure of UniProt Q9UHD2
• Elsewhere: RCSB PDB 5EP6 · PDBe 5EP6 · UniProt Q9H6S1 · UniProt Q9UHD2