1E7Q
GDP 4-keto-6-deoxy-D-mannose epimerase reductase S107A
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A1319 |
| Chain | Residue |
| A | ARG5 |
| A | VAL32 |
| A | ARG34 |
| A | GLU54 |
| A | HOH2306 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A1320 |
| Chain | Residue |
| A | HIS11 |
| A | ARG12 |
| A | ARG20 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A1321 |
| Chain | Residue |
| A | GLN237 |
| A | PRO238 |
| A | VAL271 |
| A | HOH2224 |
| A | HOH2307 |
| A | ASP198 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A1322 |
| Chain | Residue |
| A | ARG152 |
| A | PRO238 |
| A | ARG254 |
| A | VAL270 |
| A | VAL271 |
| A | PHE272 |
| A | HOH2236 |
| A | HOH2308 |
| A | HOH2309 |
| A | HOH2310 |
| site_id | AC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAP A1317 |
| Chain | Residue |
| A | GLY10 |
| A | GLY13 |
| A | MET14 |
| A | VAL15 |
| A | ARG36 |
| A | LEU39 |
| A | ASN40 |
| A | LEU41 |
| A | LEU42 |
| A | ALA62 |
| A | ALA63 |
| A | ALA64 |
| A | VAL66 |
| A | ILE86 |
| A | LEU105 |
| A | GLY106 |
| A | TYR136 |
| A | LYS140 |
| A | PRO163 |
| A | LEU166 |
| A | HOH2012 |
| A | HOH2092 |
| A | HOH2296 |
| A | HOH2297 |
| A | HOH2299 |
| A | HOH2300 |
| A | HOH2301 |
| A | HOH2302 |
| A | HOH2303 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UVW A1318 |
| Chain | Residue |
| A | GLY68 |
| A | ILE69 |
| A | VAL70 |
| A | ALA71 |
| A | SER178 |
| A | LYS262 |
| A | HOH2304 |
| A | HOH2305 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS A1323 |
| Chain | Residue |
| A | ARG21 |
| A | HIS170 |
| A | TRP311 |
| A | HOH2311 |
| A | HOH2312 |
| A | HOH2313 |
| A | HOH2314 |
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 | a catalytic site defined by CSA, PubMed 9862812, 11021971 |
| Chain | Residue | Details |
| A | CYS109 | |
| A | HIS179 | |
| A | TYR136 | |
| A | LYS140 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9862812, 11021971 |
| Chain | Residue | Details |
| A | TYR136 | |
| A | ALA107 | |
| A | LYS140 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 227 |
| Chain | Residue | Details |
| A | ALA107 | 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 |
