Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008107 | molecular_function | galactoside 2-alpha-L-fucosyltransferase activity |
A | 0016020 | cellular_component | membrane |
A | 0042546 | biological_process | cell wall biogenesis |
B | 0008107 | molecular_function | galactoside 2-alpha-L-fucosyltransferase activity |
B | 0016020 | cellular_component | membrane |
B | 0042546 | biological_process | cell wall biogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue GDP A 601 |
Chain | Residue |
A | GLY181 |
A | ALA463 |
A | GLU466 |
A | SER482 |
A | THR483 |
A | PHE484 |
A | HOH735 |
A | HOH816 |
A | HOH831 |
A | HOH934 |
A | HOH941 |
A | GLY183 |
A | ASN184 |
A | ARG366 |
A | THR416 |
A | SER417 |
A | LEU418 |
A | SER447 |
A | HIS459 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue MES A 602 |
Chain | Residue |
A | TRP553 |
A | HOH914 |
B | LEU541 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | VAL365 |
A | VAL378 |
A | GLN381 |
A | SER479 |
A | LEU499 |
A | PRO502 |
A | HOH702 |
A | HOH775 |
A | HOH1017 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 604 |
Chain | Residue |
A | ASP380 |
A | SER383 |
A | SER384 |
A | HOH899 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 605 |
Chain | Residue |
A | TYR126 |
A | LYS324 |
A | ALA325 |
A | VAL558 |
A | HOH703 |
A | HOH771 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue EDO A 606 |
Chain | Residue |
A | SER130 |
A | ILE133 |
A | SER134 |
A | ASP371 |
A | PRO374 |
A | PHE375 |
A | GLN376 |
A | ARG505 |
A | HOH982 |
A | HOH1147 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue EDO A 607 |
Chain | Residue |
A | GLU389 |
A | LYS390 |
A | ASN475 |
A | HOH701 |
A | HOH741 |
A | HOH851 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue EDO A 608 |
Chain | Residue |
A | GLU424 |
A | GLN448 |
A | HOH834 |
B | ALA420 |
B | GLU424 |
B | GLN448 |
B | EDO605 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO A 609 |
Chain | Residue |
A | ASP380 |
A | EDO610 |
A | HOH988 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 610 |
Chain | Residue |
A | EDO609 |
A | HOH886 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue GOL A 611 |
Chain | Residue |
A | TYR500 |
A | HOH728 |
A | HOH922 |
A | HOH986 |
site_id | AD3 |
Number of Residues | 19 |
Details | binding site for residue GDP B 601 |
Chain | Residue |
B | LEU182 |
B | GLY183 |
B | ASN184 |
B | ARG366 |
B | THR416 |
B | SER417 |
B | LEU418 |
B | SER447 |
B | GLN452 |
B | HIS459 |
B | ALA463 |
B | GLU466 |
B | SER482 |
B | THR483 |
B | PHE484 |
B | HOH753 |
B | HOH802 |
B | HOH828 |
B | HOH929 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue MES B 602 |
Chain | Residue |
B | HOH979 |
B | TYR247 |
B | MET250 |
B | VAL255 |
B | GLY284 |
B | ASP285 |
B | HOH750 |
B | HOH770 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue EDO B 603 |
Chain | Residue |
B | ASP380 |
B | SER383 |
B | SER384 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 604 |
Chain | Residue |
B | TYR528 |
B | CYS530 |
B | LEU541 |
B | HOH720 |
B | HOH988 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue EDO B 605 |
Chain | Residue |
A | GLN445 |
A | PRO446 |
A | SER447 |
A | GLN448 |
A | EDO608 |
B | GLU424 |
B | LYS427 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue EDO B 606 |
Chain | Residue |
B | ARG366 |
B | GLN381 |
B | SER479 |
B | LEU499 |
B | PRO502 |
B | HOH800 |
B | HOH913 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 607 |
Chain | Residue |
B | GLU283 |
B | THR287 |
B | PRO311 |
B | HOH996 |
site_id | AE1 |
Number of Residues | 7 |
Details | binding site for residue EDO B 608 |
Chain | Residue |
A | ALA352 |
B | HIS410 |
B | GLY442 |
B | HIS444 |
B | HOH701 |
B | HOH704 |
B | HOH717 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue EDO B 609 |
Chain | Residue |
B | ASP275 |
B | HIS276 |
B | TYR528 |
B | HOH794 |
B | HOH1011 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue EDO B 610 |
Chain | Residue |
A | LYS96 |
B | GLY450 |
B | TYR451 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |