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Crystal structure of the human myeloid cell activating receptor trem-1

Analyse Crystal structure of the human myeloid cell activating receptor trem-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Q8M
Type
protein
Length
484 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Triggering receptor expressed on myeloid cells 1
UniProt
Q9NP99
Ligands
GSH, SO4
Pockets
1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DTriggering receptor expressed on myeloid cells 1protein1215% helix, 53% strandQ9NP99

Ligands and binding sites

  • GSH · Glutathione · ligand · chains A, B
  • SO4 · Sulfate ion · ion · 10 copies · chains A, B, C, D

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.670.9717empty

Interfaces

3 interfaces between chains.

  • C–D · 2178 Ų buried · 24 hydrogen bonds · protein-protein
  • A–B · 2041 Ų buried · 24 hydrogen bonds · protein-protein
  • A–C · 545 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1Q8M · Crystal structure of the human myeloid cell activating receptor TREM-1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NP99 · AlphaFold monomer V2.0 prediction for triggering receptor expressed on myeloid cells 1… · a predicted model of the same protein · chain A against A, TM-score 0.88

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