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Crystal structure of the tir-domain of human myeloid differentiation primary response protein (MYD88)

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: 4DOM
Type: protein
Length: 141 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Myeloid differentiation primary response protein MYD88
UniProt: Q99836
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Myeloid differentiation primary response protein MYD88	protein	141	43% helix, 18% strand	Q99836

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.33	0.76	16	empty

Modifications

Observed in the structure: 7 modified (methylation, oxidation).

Compared structures

4DOM · 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 0.86

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 Q99836
Elsewhere: RCSB PDB 4DOM · PDBe 4DOM · UniProt Q99836

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