1KZH
Structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete 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 PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 600 |
| Chain | Residue |
| A | GLY82 |
| A | ARG146 |
| A | ARG431 |
| B | THR241 |
| B | LYS243 |
| B | TYR244 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | ASP177 |
| A | SER178 |
| A | LYS203 |
| A | HOH794 |
| A | HOH801 |
| A | ARG146 |
| A | GLY175 |
| A | ASP176 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | LYS71 |
| A | ALA72 |
| A | ASN102 |
| A | ASN104 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1600 |
| Chain | Residue |
| A | THR241 |
| A | LYS243 |
| A | TYR244 |
| B | ARG146 |
| B | ARG431 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1601 |
| Chain | Residue |
| B | SER80 |
| B | GLY81 |
| B | ARG146 |
| B | GLY175 |
| B | ASP177 |
| B | SER178 |
| B | LYS203 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1602 |
| Chain | Residue |
| B | LYS71 |
| B | ALA72 |
| B | ASN102 |
| B | ASN104 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1603 |
| Chain | Residue |
| A | HIS424 |
| A | PHE425 |
| A | HOH759 |
| A | HOH783 |
| B | HIS424 |
| B | PHE425 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1604 |
| Chain | Residue |
| B | LYS23 |
| B | ASP24 |
| B | ASN27 |
| B | GLU62 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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_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 |
| site_id | SWS_FT_FI8 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12015149 |
| Chain | Residue | Details |
| A | THR204 | |
| A | ASP206 | |
| A | GLY82 | |
| A | LYS203 | |
| A | ARG146 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12015149 |
| 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 |
