3DRW
Crystal Structure of a Phosphofructokinase from Pyrococcus horikoshii OT3 with AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006000 | biological_process | fructose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008443 | molecular_function | phosphofructokinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0043844 | molecular_function | ADP-specific phosphofructokinase activity |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006000 | biological_process | fructose metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008443 | molecular_function | phosphofructokinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0043844 | molecular_function | ADP-specific phosphofructokinase activity |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AMP A 1484 |
| Chain | Residue |
| A | THR336 |
| A | HOH1656 |
| A | HOH1730 |
| A | THR337 |
| A | ARG420 |
| A | LEU421 |
| A | VAL422 |
| A | LEU431 |
| A | ILE435 |
| A | NA1486 |
| A | HOH1641 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 1485 |
| Chain | Residue |
| A | THR104 |
| A | ARG369 |
| A | ILE375 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 1486 |
| Chain | Residue |
| A | LEU431 |
| A | GLY432 |
| A | AMP1484 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP B 1485 |
| Chain | Residue |
| B | HIS335 |
| B | THR336 |
| B | THR337 |
| B | THR419 |
| B | ARG420 |
| B | LEU421 |
| B | VAL422 |
| B | LEU431 |
| B | GLY432 |
| B | ILE435 |
| B | HOH1707 |
| B | HOH1785 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00561 |
| Chain | Residue | Details |
| A | ASP433 | |
| B | ASP433 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00561 |
| Chain | Residue | Details |
| A | GLU260 | |
| A | GLU290 | |
| A | ASP433 | |
| B | GLU260 | |
| B | GLU290 | |
| B | ASP433 |
