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 | 0016740 | molecular_function | transferase 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 | 0016740 | molecular_function | transferase 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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A796","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01980","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01980","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of a novel fructose 1,6-bisphosphate and AlF(3) containing pyrophosphate-dependent phosphofructo-1-kinase complex from Borrelia burgdorferi.","authors":["Wang M.","Grum-Tokars V."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of a novel fructose 1,6-bisphosphate and AlF(3) containing pyrophosphate-dependent phosphofructo-1-kinase complex from Borrelia burgdorferi.","authors":["Wang M.","Grum-Tokars V."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A796","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01980","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_01980","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of a novel fructose 1,6-bisphosphate and AlF(3) containing pyrophosphate-dependent phosphofructo-1-kinase complex from Borrelia burgdorferi.","authors":["Wang M.","Grum-Tokars V."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Site: {"description":"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","evidences":[{"source":"HAMAP-Rule","id":"MF_01980","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12015149","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Site: {"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"source":"HAMAP-Rule","id":"MF_01980","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12015149","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
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 |