1MC3
CRYSTAL STRUCTURE OF RFFH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008879 | molecular_function | glucose-1-phosphate thymidylyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009246 | biological_process | enterobacterial common antigen biosynthetic process |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ASP108 |
| A | ASP223 |
| A | TTP294 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ASP108 |
| B | ASP223 |
| B | TTP295 |
| B | HOH326 |
| B | HOH380 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TTP A 294 |
| Chain | Residue |
| A | GLY8 |
| A | GLY9 |
| A | SER10 |
| A | GLY11 |
| A | THR12 |
| A | ARG13 |
| A | LYS23 |
| A | GLN24 |
| A | GLN80 |
| A | PRO83 |
| A | ASP84 |
| A | GLY85 |
| A | LEU86 |
| A | GLY107 |
| A | ASP108 |
| A | GLU194 |
| A | MG301 |
| A | HOH346 |
| A | HOH379 |
| A | HOH466 |
| A | LEU6 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE TTP B 295 |
| Chain | Residue |
| B | LEU6 |
| B | GLY8 |
| B | GLY9 |
| B | SER10 |
| B | GLY11 |
| B | THR12 |
| B | ARG13 |
| B | LYS23 |
| B | GLN24 |
| B | GLN80 |
| B | PRO83 |
| B | ASP84 |
| B | GLY85 |
| B | LEU86 |
| B | GLY107 |
| B | ASP108 |
| B | MG302 |
| B | HOH326 |
| B | HOH378 |
| B | HOH380 |
| B | HOH441 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12171937 |
| Chain | Residue | Details |
| A | ASP108 | |
| A | ASP223 | |
| B | ASP108 | |
| B | ASP223 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| A | ARG13 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| B | ARG13 |
