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Crystal structure of human alpha 1,6-fucosyltransferase, FUT8

Analyse Crystal structure of human alpha 1,6-fucosyltransferase, FUT8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2DE0
Type: protein
Length: 460 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-(1,6)-fucosyltransferase
EC: 2.4.1.68
UniProt: Q9BYC5
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Alpha-(1,6)-fucosyltransferase (EC 2.4.1.68)	protein	460	46% helix, 16% strand	Q9BYC5

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	256	0.57	0.78	38	empty
2	355	0.55	0.74	30	empty
3	171	0.55	0.80	26	empty
4	145	0.42	0.75	26	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2DE0 · Crystal structure of human alpha 1,6-fucosyltransferase, FUT8 · the same entry in another collection · chain X against X, TM-score 1.00
Q9BYC5 · AlphaFold monomer V2.0 prediction for alpha-(1,6)-fucosyltransferase (Q9BYC5) · a predicted model of the same protein · chain X against A, TM-score 0.97

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 Q9BYC5
Elsewhere: RCSB PDB 2DE0 · PDBe 2DE0 · UniProt Q9BYC5

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