Research workbench
Crystal structure of human alpha 1,6-fucosyltransferase, FUT8 in its apo-form
Analyse Crystal structure of human alpha 1,6-fucosyltransferase, FUT8 in its apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VLE
- Type
- protein
- Length
- 918 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-(1,6)-fucosyltransferase
- EC
- 2.4.1.68
- UniProt
- Q9BYC5
- Ligands
- SO4
- Pockets
- 15 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-(1,6)-fucosyltransferase (EC 2.4.1.68) | protein | 460 | 45% helix, 17% strand | Q9BYC5 |
| B | Alpha-(1,6)-fucosyltransferase (EC 2.4.1.68) | protein | 458 | 45% helix, 17% strand | Q9BYC5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1030 | 0.85 | 0.86 | 86 | empty |
| 2 | 1180 | 0.83 | 0.84 | 101 | empty |
| 3 | 149 | 0.56 | 0.81 | 21 | empty |
| 4 | 139 | 0.54 | 0.81 | 20 | empty |
| 5 | 77 | 0.46 | 0.82 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3336 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6VLE · Crystal structure of human alpha 1,6-fucosyltransferase, FUT8 in its Apo-form · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BYC5 · AlphaFold monomer V2.0 prediction for alpha-(1,6)-fucosyltransferase (Q9BYC5) · a predicted model of the same protein · chain B 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 6VLE · PDBe 6VLE · UniProt Q9BYC5
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