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Crystal structure of the ubiquitin-like domain of human TBK1

Analyse Crystal structure of the ubiquitin-like domain of human TBK1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EFO
Type: protein
Length: 171 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SERINE/THREONINE-protein kinase TBK1
EC: 2.7.11.1
UniProt: Q9UHD2
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SERINE/THREONINE-protein kinase TBK1 (EC 2.7.11.1)	protein	89	27% helix, 37% strand	Q9UHD2
B	SERINE/THREONINE-protein kinase TBK1 (EC 2.7.11.1)	protein	82	26% helix, 38% strand	Q9UHD2

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.37	0.77	21	empty
2	66	0.36	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 437 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

4EFO · Crystal structure of the ubiquitin-like domain of human TBK1 · the same entry in another collection · chain A against A, TM-score 1.00
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 0.95

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 Q9UHD2
Elsewhere: RCSB PDB 4EFO · PDBe 4EFO · UniProt Q9UHD2

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