3F5M
Crystal Structure of ATP-Bound Phosphofructokinase from Trypanosoma brucei
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 | 0006002 | biological_process | fructose 6-phosphate metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0016301 | molecular_function | kinase 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 | 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 | 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 | 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 | 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 | 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 | 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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03186 |
Chain | Residue | Details |
A | ASP229 | |
B | ASP229 | |
C | ASP229 | |
D | ASP229 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:19084537 |
Chain | Residue | Details |
A | GLY107 | |
C | ARG173 | |
C | GLY198 | |
C | SER341 | |
D | GLY107 | |
D | ARG173 | |
D | GLY198 | |
D | SER341 | |
A | ARG173 | |
A | GLY198 | |
A | SER341 | |
B | GLY107 | |
B | ARG173 | |
B | GLY198 | |
B | SER341 | |
C | GLY107 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03186 |
Chain | Residue | Details |
A | ASP199 | |
B | TYR380 | |
C | ASP199 | |
C | THR227 | |
C | MET272 | |
C | GLU325 | |
C | TYR380 | |
D | ASP199 | |
D | THR227 | |
D | MET272 | |
D | GLU325 | |
A | THR227 | |
D | TYR380 | |
A | MET272 | |
A | GLU325 | |
A | TYR380 | |
B | ASP199 | |
B | THR227 | |
B | MET272 | |
B | GLU325 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19084537 |
Chain | Residue | Details |
A | LYS226 | |
B | LYS226 | |
C | LYS226 | |
D | LYS226 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Important for substrate specificity; cannot use PPi as phosphoryl donor => ECO:0000255|HAMAP-Rule:MF_03186 |
Chain | Residue | Details |
A | GLY200 | |
B | GLY200 | |
C | GLY200 | |
D | GLY200 |
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 |