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Crystal structure of the tir domain of human TLR1 (crystallised with ZN2+ ions)

Analyse Crystal structure of the tir domain of human TLR1 (crystallised with ZN2+ ions) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NUW
Type
protein
Length
159 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Toll-like receptor 1
EC
3.2.2.6
UniProt
Q15399
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AToll-like receptor 1 (EC 3.2.2.6)protein15944% helix, 15% strandQ15399

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.400.7719empty
2670.320.7515empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7NUW · Crystal structure of the TIR domain of human TLR1 (crystallised with Zn2+ ions) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q15399 · AlphaFold monomer V2.0 prediction for toll-like receptor 1 (Q15399) · a predicted model of the same protein · chain A against A, TM-score 0.90

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