2F48
Crystal Structure of A Novel Fructose 1,6-Bisphosphate and AlF3 containing Pyrophosphate-dependent Phosphofructo-1-kinase Complex from Borrelia burgdorferi
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008443 | molecular_function | phosphofructokinase activity |
| A | 0009749 | biological_process | response to glucose |
| A | 0016301 | molecular_function | kinase activity |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047334 | molecular_function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008443 | molecular_function | phosphofructokinase activity |
| B | 0009749 | biological_process | response to glucose |
| B | 0016301 | molecular_function | kinase activity |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047334 | molecular_function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity |
| B | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980 |
| Chain | Residue | Details |
| A | ASP206 | |
| B | ASP206 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5 |
| Chain | Residue | Details |
| A | GLY82 | |
| A | LYS243 | |
| B | GLY82 | |
| B | LYS243 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0000269|Ref.5 |
| Chain | Residue | Details |
| A | ARG146 | |
| B | ARG146 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A796, ECO:0000255|HAMAP-Rule:MF_01980 |
| Chain | Residue | Details |
| A | ASP176 | |
| B | ASP176 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000269|Ref.5 |
| Chain | Residue | Details |
| A | THR204 | |
| A | MET251 | |
| A | GLU312 | |
| A | TYR428 | |
| B | THR204 | |
| B | MET251 | |
| B | GLU312 | |
| B | TYR428 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149 |
| Chain | Residue | Details |
| A | ASP177 | |
| B | ASP177 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi => ECO:0000255|HAMAP-Rule:MF_01980, ECO:0000305|PubMed:12015149 |
| Chain | Residue | Details |
| A | LYS203 | |
| B | LYS203 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1kzh |
| Chain | Residue | Details |
| A | THR204 | |
| A | ASP206 | |
| A | GLY82 | |
| A | LYS203 | |
| A | ARG146 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1kzh |
| Chain | Residue | Details |
| B | THR204 | |
| B | ASP206 | |
| B | GLY82 | |
| B | LYS203 | |
| B | ARG146 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 653 |
| Chain | Residue | Details |
| A | GLY82 | electrostatic stabiliser, polar interaction |
| A | ARG146 | electrostatic stabiliser, polar interaction |
| A | ASP177 | polar interaction |
| A | LYS203 | electrostatic stabiliser, polar interaction |
| A | THR204 | electrostatic stabiliser, polar interaction |
| A | ASP206 | activator, electrostatic stabiliser, polar interaction, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 653 |
| Chain | Residue | Details |
| B | GLY82 | electrostatic stabiliser, polar interaction |
| B | ARG146 | electrostatic stabiliser, polar interaction |
| B | ASP177 | polar interaction |
| B | LYS203 | electrostatic stabiliser, polar interaction |
| B | THR204 | electrostatic stabiliser, polar interaction |
| B | ASP206 | activator, electrostatic stabiliser, polar interaction, proton acceptor, proton donor |
