7AGK
Crystal structure of E. coli SF kinase (YihV) in complex with product sulfofructose phosphate (SFP)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0061594 | molecular_function | 6-deoxy-6-sulfofructose kinase activity |
| A | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
| B | 0005829 | cellular_component | cytosol |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0061594 | molecular_function | 6-deoxy-6-sulfofructose kinase activity |
| B | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
| C | 0005829 | cellular_component | cytosol |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| C | 0046835 | biological_process | carbohydrate phosphorylation |
| C | 0061594 | molecular_function | 6-deoxy-6-sulfofructose kinase activity |
| C | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
| D | 0005829 | cellular_component | cytosol |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016772 | molecular_function | transferase activity, transferring phosphorus-containing groups |
| D | 0046835 | biological_process | carbohydrate phosphorylation |
| D | 0061594 | molecular_function | 6-deoxy-6-sulfofructose kinase activity |
| D | 1902777 | biological_process | 6-sulfoquinovose(1-) catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue RAH A 401 |
| Chain | Residue |
| A | VAL11 |
| A | ASP162 |
| A | GLY241 |
| A | ASP244 |
| B | LYS27 |
| A | ASP13 |
| A | GLY38 |
| A | GLY39 |
| A | PRO40 |
| A | SER95 |
| A | ILE107 |
| A | ASN109 |
| A | ARG138 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue RAH B 401 |
| Chain | Residue |
| A | LYS27 |
| B | VAL11 |
| B | ASP13 |
| B | GLY38 |
| B | GLY39 |
| B | PRO40 |
| B | SER95 |
| B | ILE107 |
| B | ASN109 |
| B | ARG138 |
| B | ASP162 |
| B | ASP244 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue RAH C 401 |
| Chain | Residue |
| C | VAL11 |
| C | ASP13 |
| C | GLY38 |
| C | GLY39 |
| C | PRO40 |
| C | SER95 |
| C | ASN109 |
| C | ARG138 |
| C | ASP162 |
| C | ASP244 |
| D | LYS27 |
Functional Information from PROSITE/UniProt
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDvfhGALA |
| Chain | Residue | Details |
| D | ASP238-ALA251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00999","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33791429","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7AG6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AGK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00999","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33791429","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7AG6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7AGH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
