6VLG
Crystal structure of mouse alpha 1,6-fucosyltransferase, FUT8 bound to GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008424 | molecular_function | glycoprotein 6-alpha-L-fucosyltransferase activity |
| A | 0009101 | biological_process | glycoprotein biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0032580 | cellular_component | Golgi cisterna membrane |
| B | 0008424 | molecular_function | glycoprotein 6-alpha-L-fucosyltransferase activity |
| B | 0009101 | biological_process | glycoprotein biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0032580 | cellular_component | Golgi cisterna membrane |
| C | 0008424 | molecular_function | glycoprotein 6-alpha-L-fucosyltransferase activity |
| C | 0009101 | biological_process | glycoprotein biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0032580 | cellular_component | Golgi cisterna membrane |
| D | 0008424 | molecular_function | glycoprotein 6-alpha-L-fucosyltransferase activity |
| D | 0009101 | biological_process | glycoprotein biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0032580 | cellular_component | Golgi cisterna membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue GDP A 601 |
| Chain | Residue |
| A | GLY219 |
| A | THR408 |
| A | ILE432 |
| A | ALA436 |
| A | ARG441 |
| A | GLY449 |
| A | VAL450 |
| A | ASP453 |
| A | SER469 |
| A | GLN470 |
| A | VAL471 |
| A | TYR220 |
| A | HOH714 |
| A | HOH730 |
| A | HOH733 |
| A | HOH734 |
| A | GLY221 |
| A | CYS222 |
| A | TYR250 |
| A | HIS363 |
| A | ARG365 |
| A | LYS369 |
| A | ALA407 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | HIS298 |
| D | LYS541 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue GDP B 601 |
| Chain | Residue |
| B | GLY219 |
| B | TYR220 |
| B | GLY221 |
| B | CYS222 |
| B | TYR250 |
| B | HIS363 |
| B | ARG365 |
| B | LYS369 |
| B | ALA407 |
| B | THR408 |
| B | ILE432 |
| B | ALA436 |
| B | ARG441 |
| B | GLY449 |
| B | VAL450 |
| B | ASP453 |
| B | SER469 |
| B | GLN470 |
| B | VAL471 |
| B | HOH726 |
| B | HOH738 |
| B | HOH740 |
| B | HOH784 |
| B | HOH800 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 602 |
| Chain | Residue |
| B | HIS298 |
| B | PRO299 |
| B | ARG300 |
| C | LYS541 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue GDP C 601 |
| Chain | Residue |
| C | GLY219 |
| C | TYR220 |
| C | GLY221 |
| C | CYS222 |
| C | TYR250 |
| C | HIS363 |
| C | ARG365 |
| C | LYS369 |
| C | ALA407 |
| C | THR408 |
| C | ILE432 |
| C | ALA436 |
| C | ARG441 |
| C | GLY449 |
| C | VAL450 |
| C | ASP453 |
| C | SER468 |
| C | SER469 |
| C | GLN470 |
| C | VAL471 |
| C | HOH707 |
| C | HOH716 |
| C | HOH776 |
| C | HOH778 |
| C | HOH802 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue PG4 C 602 |
| Chain | Residue |
| C | ARG118 |
| C | HOH817 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 603 |
| Chain | Residue |
| C | LEU297 |
| C | HIS298 |
| C | PRO299 |
| C | ARG300 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | binding site for residue GDP D 601 |
| Chain | Residue |
| D | VAL450 |
| D | ASP453 |
| D | SER469 |
| D | GLN470 |
| D | VAL471 |
| D | HOH718 |
| D | HOH742 |
| D | HOH744 |
| D | HOH830 |
| D | GLY219 |
| D | TYR220 |
| D | GLY221 |
| D | CYS222 |
| D | TYR250 |
| D | HIS363 |
| D | ARG365 |
| D | LYS369 |
| D | ALA407 |
| D | THR408 |
| D | ASP409 |
| D | ILE432 |
| D | ALA436 |
| D | ARG441 |
| D | GLY449 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue PGE D 602 |
| Chain | Residue |
| D | ARG118 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 603 |
| Chain | Residue |
| D | HIS298 |
| D | PRO299 |
| D | ARG300 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1148 |
| Details | Domain: {"description":"GT23","evidences":[{"source":"PROSITE-ProRule","id":"PRU00992","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 244 |
| Details | Domain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Region: {"description":"Important for donor substrate binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Motif: {"description":"SH3-binding","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
