1PFK
CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005945 | cellular_component | 6-phosphofructokinase complex |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006007 | biological_process | glucose catabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008443 | molecular_function | phosphofructokinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019003 | molecular_function | GDP binding |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0032553 | molecular_function | ribonucleotide binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070095 | molecular_function | fructose-6-phosphate binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005945 | cellular_component | 6-phosphofructokinase complex |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006007 | biological_process | glucose catabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008443 | molecular_function | phosphofructokinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019003 | molecular_function | GDP binding |
| B | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| B | 0032553 | molecular_function | ribonucleotide binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0070095 | molecular_function | fructose-6-phosphate binding |
Functional Information from PROSITE/UniProt
| site_id | PS00433 |
| Number of Residues | 19 |
| Details | PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RatvlGHiQRGGspvpyDR |
| Chain | Residue | Details |
| A | ARG243-ARG261 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2953977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2975709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2975709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2975709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P00512","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 2527305 |
| Chain | Residue | Details |
| A | GLY11 | |
| A | ASP127 | |
| A | THR125 | |
| A | ARG72 | |
| A | ARG171 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 2527305 |
| Chain | Residue | Details |
| B | GLY11 | |
| B | ASP127 | |
| B | THR125 | |
| B | ARG72 | |
| B | ARG171 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 365 |
| Chain | Residue | Details |
| A | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG72 | electrostatic stabiliser |
| A | ASP103 | metal ligand |
| A | THR125 | electrostatic stabiliser |
| A | ASP127 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| A | ASP129 | hydrogen bond acceptor, increase acidity, increase basicity |
| A | ARG171 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 365 |
| Chain | Residue | Details |
| B | GLY11 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG72 | electrostatic stabiliser |
| B | ASP103 | metal ligand |
| B | THR125 | electrostatic stabiliser |
| B | ASP127 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| B | ASP129 | hydrogen bond acceptor, increase acidity, increase basicity |
| B | ARG171 | electrostatic stabiliser |
