1BSV
GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009226 | biological_process | nucleotide-sugar biosynthetic process |
| A | 0009242 | biological_process | colanic acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042351 | biological_process | 'de novo' GDP-L-fucose biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050577 | molecular_function | GDP-L-fucose synthase activity |
| A | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP A 350 |
| Chain | Residue |
| A | ARG12 |
| A | ALA64 |
| A | VAL66 |
| A | ILE86 |
| A | LEU105 |
| A | GLY106 |
| A | TYR136 |
| A | LYS140 |
| A | THR164 |
| A | HOH437 |
| A | HOH478 |
| A | GLY13 |
| A | HOH483 |
| A | HOH484 |
| A | HOH485 |
| A | HOH488 |
| A | MET14 |
| A | VAL15 |
| A | ARG36 |
| A | LEU39 |
| A | ASN40 |
| A | LEU41 |
| A | ALA63 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00956","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11021971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00956","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11021971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9817848","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9862812","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00956","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lowers pKa of active site Tyr"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | CYS109 | |
| A | HIS179 | |
| A | TYR136 | |
| A | LYS140 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR136 | |
| A | SER107 | |
| A | LYS140 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 227 |
| Chain | Residue | Details |
| A | SER107 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, increase basicity, proton acceptor, proton donor |
| A | SER108 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS109 | electrostatic stabiliser, hydrogen bond donor, proton acceptor |
| A | TYR136 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | LYS140 | electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
| A | HIS179 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
