Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0005829 | cellular_component | cytosol |
| A | 0008831 | molecular_function | dTDP-4-dehydrorhamnose reductase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009243 | biological_process | O antigen biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | HOH908 |
| A | HOH908 |
| A | HOH909 |
| A | HOH909 |
| A | HOH910 |
| A | HOH910 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP A 901 |
| Chain | Residue |
| A | VAL31 |
| A | GLY38 |
| A | ASP39 |
| A | PHE40 |
| A | SER41 |
| A | ALA61 |
| A | ALA62 |
| A | ALA63 |
| A | THR65 |
| A | LEU80 |
| A | TYR102 |
| A | SER103 |
| A | THR104 |
| A | TYR128 |
| A | LYS132 |
| A | THR151 |
| A | VAL154 |
| A | GLN174 |
| A | TRH601 |
| A | HOH904 |
| A | HOH907 |
| A | HOH978 |
| A | HOH994 |
| A | GLY10 |
| A | GLN11 |
| A | VAL12 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE TRH A 601 |
| Chain | Residue |
| A | VAL67 |
| A | THR104 |
| A | ASP105 |
| A | TYR106 |
| A | TYR128 |
| A | SER152 |
| A | TRP153 |
| A | PHE162 |
| A | SER177 |
| A | VAL178 |
| A | ILE179 |
| A | GLN182 |
| A | TRP223 |
| A | ARG260 |
| A | NDP901 |
| A | HOH951 |
| A | HOH952 |
| A | HOH988 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1N2S","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KC1","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KC3","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Could provide a fine-tuning to achieve optimal pKa matching between active site and substrate","evidences":[{"source":"PubMed","id":"12057193","evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | THR104 | |
| A | TYR106 | |
| A | TYR128 | |
| A | LYS132 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | THR104 | |
| A | LYS132 | |
| A | TYR128 | |
