3F5M
Crystal Structure of ATP-Bound Phosphofructokinase from Trypanosoma brucei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0020015 | cellular_component | glycosome |
| A | 0042301 | molecular_function | phosphate ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0020015 | cellular_component | glycosome |
| B | 0042301 | molecular_function | phosphate ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003872 | molecular_function | 6-phosphofructokinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0020015 | cellular_component | glycosome |
| C | 0042301 | molecular_function | phosphate ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003872 | molecular_function | 6-phosphofructokinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0020015 | cellular_component | glycosome |
| D | 0042301 | molecular_function | phosphate ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A1001 |
| Chain | Residue |
| A | GLY106 |
| A | THR201 |
| A | GLY204 |
| A | LYS226 |
| A | SER341 |
| A | ASN343 |
| A | MG1002 |
| A | GLY107 |
| A | TYR139 |
| A | ARG173 |
| A | GLY174 |
| A | PRO175 |
| A | GLY198 |
| A | ASP199 |
| A | GLY200 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A1002 |
| Chain | Residue |
| A | ASN343 |
| A | ATP1001 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 488 |
| Chain | Residue |
| A | ASN291 |
| A | ILE292 |
| A | CYS293 |
| A | LEU308 |
| A | THR451 |
| A | VAL452 |
| A | HOH556 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 489 |
| Chain | Residue |
| A | ARG448 |
| A | THR451 |
| A | VAL452 |
| A | ASP453 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 490 |
| Chain | Residue |
| A | ALA259 |
| A | VAL260 |
| A | ALA262 |
| A | ARG317 |
| A | SER318 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP B1001 |
| Chain | Residue |
| B | GLY106 |
| B | GLY107 |
| B | TYR139 |
| B | ARG173 |
| B | GLY174 |
| B | PRO175 |
| B | GLY198 |
| B | ASP199 |
| B | GLY200 |
| B | THR201 |
| B | ARG203 |
| B | GLY204 |
| B | LYS226 |
| B | SER341 |
| B | ASN343 |
| B | HOH557 |
| B | MG1002 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B1002 |
| Chain | Residue |
| B | ASN343 |
| B | HOH588 |
| B | ATP1001 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 488 |
| Chain | Residue |
| B | VAL260 |
| B | ALA262 |
| B | ARG317 |
| B | SER318 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP C1001 |
| Chain | Residue |
| C | GLY106 |
| C | GLY107 |
| C | TYR139 |
| C | ARG173 |
| C | GLY174 |
| C | PRO175 |
| C | GLY198 |
| C | ASP199 |
| C | GLY200 |
| C | THR201 |
| C | ARG203 |
| C | GLY204 |
| C | LYS226 |
| C | SER341 |
| C | ASN343 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 488 |
| Chain | Residue |
| C | ILE292 |
| C | CYS293 |
| C | ASN298 |
| C | THR451 |
| C | NA490 |
| C | HOH549 |
| C | HOH559 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 489 |
| Chain | Residue |
| C | GLY106 |
| C | GLY107 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 490 |
| Chain | Residue |
| C | ARG448 |
| C | THR451 |
| C | VAL452 |
| C | ASP453 |
| C | GOL488 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP D1001 |
| Chain | Residue |
| D | ASN343 |
| D | HOH488 |
| D | HOH575 |
| D | MG1002 |
| D | GLY107 |
| D | TYR139 |
| D | ARG173 |
| D | GLY174 |
| D | PRO175 |
| D | GLY198 |
| D | ASP199 |
| D | GLY200 |
| D | THR201 |
| D | ARG203 |
| D | GLY204 |
| D | LYS226 |
| D | SER341 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D1002 |
| Chain | Residue |
| D | ASN343 |
| D | ATP1001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19084537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19084537","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for substrate specificity; cannot use PPi as phosphoryl donor","evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| A | GLY107 | |
| A | ASP229 | |
| A | ARG274 | |
| A | ARG173 | |
| A | THR227 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| B | GLY107 | |
| B | ASP229 | |
| B | ARG274 | |
| B | ARG173 | |
| B | THR227 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| C | GLY107 | |
| C | ASP229 | |
| C | ARG274 | |
| C | ARG173 | |
| C | THR227 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| D | GLY107 | |
| D | ASP229 | |
| D | ARG274 | |
| D | ARG173 | |
| D | THR227 |
| site_id | CSA5 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| A | LYS226 | |
| A | GLY107 | |
| A | ASP229 | |
| A | ARG173 | |
| A | THR227 |
| site_id | CSA6 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| B | LYS226 | |
| B | GLY107 | |
| B | ASP229 | |
| B | ARG173 | |
| B | THR227 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| C | LYS226 | |
| C | GLY107 | |
| C | ASP229 | |
| C | ARG173 | |
| C | THR227 |
| site_id | CSA8 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1pfk |
| Chain | Residue | Details |
| D | LYS226 | |
| D | GLY107 | |
| D | ASP229 | |
| D | ARG173 | |
| D | THR227 |
