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 | 0000287 | molecular_function | magnesium ion binding |
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 | 0016208 | molecular_function | AMP binding |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
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 | 0046872 | molecular_function | metal ion binding |
A | 0048029 | molecular_function | monosaccharide binding |
A | 0051289 | biological_process | protein homotetramerization |
A | 0061621 | biological_process | canonical glycolysis |
A | 0070095 | molecular_function | fructose-6-phosphate binding |
B | 0000287 | molecular_function | magnesium ion binding |
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 | 0016208 | molecular_function | AMP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
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 | 0046872 | molecular_function | metal ion binding |
B | 0048029 | molecular_function | monosaccharide 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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:2953977, ECO:0000269|PubMed:2975709 |
Chain | Residue | Details |
A | ASP127 | |
B | ASP127 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:2975709 |
Chain | Residue | Details |
A | GLY11 | |
B | ARG21 | |
B | ARG54 | |
B | ARG72 | |
B | GLY102 | |
B | ASP103 | |
B | ARG162 | |
B | ARG243 | |
A | ARG21 | |
A | ARG54 | |
A | ARG72 | |
A | GLY102 | |
A | ASP103 | |
A | ARG162 | |
A | ARG243 | |
B | GLY11 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339, ECO:0000269|PubMed:2975709 |
Chain | Residue | Details |
A | THR125 | |
B | LYS213 | |
B | GLU222 | |
B | HIS249 | |
A | ARG154 | |
A | GLY185 | |
A | LYS213 | |
A | GLU222 | |
A | HIS249 | |
B | THR125 | |
B | ARG154 | |
B | GLY185 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P00512, ECO:0000255|HAMAP-Rule:MF_00339 |
Chain | Residue | Details |
A | MET169 | |
A | LYS211 | |
B | MET169 | |
B | LYS211 |
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 |