Research workbench
Crystal structure of mouse alpha 1,6-fucosyltransferase, FUT8 bound to GDP
Analyse Crystal structure of mouse alpha 1,6-fucosyltransferase, FUT8 bound to GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VLG
- Type
- protein
- Length
- 1,872 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9WTS2
- Ligands
- GDP, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 468 | — | Q9WTS2 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 4 copies · chains A, D, B, C
- PG4 · Tetraethylene glycol · additive · chains C
- PGE · Triethylene glycol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VLG · Crystal structure of mouse alpha 1,6-fucosyltransferase, FUT8 bound to GDP · the same entry in another collection · chain D against D, TM-score 1.00
- Q9WTS2 · AlphaFold monomer V2.0 prediction for alpha-(1,6)-fucosyltransferase (Q9WTS2) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q9WTS2
- Elsewhere: RCSB PDB 6VLG · PDBe 6VLG · UniProt Q9WTS2
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