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Crystal structure of the tir domain of human myeloid differentiation primary response protein 88.

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

PDB
4EO7
Type
protein
Length
144 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Myeloid differentiation primary response protein MYD88
UniProt
Q99836
Ligands
MG
Pockets
2 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMyeloid differentiation primary response protein MYD88protein14442% helix, 18% strandQ99836

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.350.7814empty
2620.290.7413empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 4EO7 · Crystal structure of the TIR domain of human myeloid differentiation primary response… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q99836 · AlphaFold monomer V2.0 prediction for myeloid differentiation primary response protein… · a predicted model of the same protein · chain A against A, TM-score 0.84

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