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Crystal structure of the tir domain of human TLR1

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

PDB: 1FYV
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Toll-like receptor 1
UniProt: Q15399
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Toll-like receptor 1	protein	161	40% helix, 14% strand	Q15399

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	93	0.36	0.75	18	empty
2	59	0.29	0.74	14	empty

Modifications

Observed in the structure: 2 modified, 1 disulfide (engineered, disulfide).

Compared structures

1FYV · Crystal structure of the tir domain of human TLR1 · 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 0.88

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 Q15399
Elsewhere: RCSB PDB 1FYV · PDBe 1FYV · UniProt Q15399

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