1K6M
Crystal Structure of Human Liver 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
A | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006000 | biological_process | fructose metabolic process |
A | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019900 | molecular_function | kinase binding |
A | 0031100 | biological_process | animal organ regeneration |
A | 0032868 | biological_process | response to insulin |
A | 0033762 | biological_process | response to glucagon |
A | 0042594 | biological_process | response to starvation |
A | 0042802 | molecular_function | identical protein binding |
A | 0043540 | cellular_component | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0051384 | biological_process | response to glucocorticoid |
A | 0051591 | biological_process | response to cAMP |
A | 0070095 | molecular_function | fructose-6-phosphate binding |
A | 1904539 | biological_process | negative regulation of glycolytic process through fructose-6-phosphate |
A | 1904540 | biological_process | positive regulation of glycolytic process through fructose-6-phosphate |
B | 0003824 | molecular_function | catalytic activity |
B | 0003873 | molecular_function | 6-phosphofructo-2-kinase activity |
B | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006000 | biological_process | fructose metabolic process |
B | 0006003 | biological_process | fructose 2,6-bisphosphate metabolic process |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019900 | molecular_function | kinase binding |
B | 0031100 | biological_process | animal organ regeneration |
B | 0032868 | biological_process | response to insulin |
B | 0033762 | biological_process | response to glucagon |
B | 0042594 | biological_process | response to starvation |
B | 0042802 | molecular_function | identical protein binding |
B | 0043540 | cellular_component | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex |
B | 0046835 | biological_process | carbohydrate phosphorylation |
B | 0051384 | biological_process | response to glucocorticoid |
B | 0051591 | biological_process | response to cAMP |
B | 0070095 | molecular_function | fructose-6-phosphate binding |
B | 1904539 | biological_process | negative regulation of glycolytic process through fructose-6-phosphate |
B | 1904540 | biological_process | positive regulation of glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 501 |
Chain | Residue |
A | ARG257 |
A | HIS258 |
A | ASN264 |
A | ARG307 |
A | GLU327 |
A | HIS392 |
A | GLN393 |
A | HOH742 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 502 |
Chain | Residue |
A | ARG352 |
A | LYS356 |
A | TYR367 |
A | GLN393 |
A | ARG397 |
A | HOH637 |
A | HOH639 |
A | HOH664 |
A | TYR338 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AGS A 503 |
Chain | Residue |
A | ALA51 |
A | ARG52 |
A | GLY53 |
A | LYS54 |
A | THR55 |
A | TYR56 |
A | ASP130 |
A | SER158 |
A | ASN169 |
A | GLN172 |
A | VAL173 |
A | LYS174 |
A | VAL222 |
A | VAL248 |
A | TYR429 |
A | HOH603 |
A | HOH658 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 501 |
Chain | Residue |
B | ARG257 |
B | HIS258 |
B | ASN264 |
B | ARG307 |
B | GLU327 |
B | HIS392 |
B | GLN393 |
B | HOH613 |
B | HOH636 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 B 502 |
Chain | Residue |
B | TYR338 |
B | ARG352 |
B | LYS356 |
B | TYR367 |
B | GLN393 |
B | ARG397 |
B | HOH608 |
B | HOH734 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AGS B 503 |
Chain | Residue |
B | ALA51 |
B | ARG52 |
B | GLY53 |
B | LYS54 |
B | THR55 |
B | TYR56 |
B | ASP130 |
B | SER158 |
B | ASN169 |
B | GLN172 |
B | VAL173 |
B | LYS174 |
B | VAL222 |
B | TYR429 |
B | HOH614 |
B | HOH628 |
B | HOH646 |
B | HOH647 |
B | HOH684 |
Functional Information from PROSITE/UniProt
site_id | PS00175 |
Number of Residues | 10 |
Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN |
Chain | Residue | Details |
A | LEU255-ASN264 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255 |
Chain | Residue | Details |
A | ASP130 | |
A | CYS160 | |
B | ASP130 | |
B | CYS160 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P07953 |
Chain | Residue | Details |
A | HIS258 | |
B | HIS258 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P07953 |
Chain | Residue | Details |
A | GLU327 | |
B | GLU327 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12379646 |
Chain | Residue | Details |
A | GLY48 | |
A | ASN169 | |
A | TYR429 | |
B | GLY48 | |
B | ASN169 | |
B | TYR429 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q16875 |
Chain | Residue | Details |
A | ARG81 | |
A | ARG307 | |
B | ARG81 | |
B | ARG104 | |
B | THR132 | |
B | ARG138 | |
B | LYS174 | |
B | ARG195 | |
B | TYR199 | |
B | ARG257 | |
B | ASN264 | |
A | ARG104 | |
B | ARG307 | |
A | THR132 | |
A | ARG138 | |
A | LYS174 | |
A | ARG195 | |
A | TYR199 | |
A | ARG257 | |
A | ASN264 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P07953 |
Chain | Residue | Details |
A | GLY270 | |
B | TYR338 | |
B | PHE349 | |
B | ARG352 | |
B | LYS356 | |
B | TYR367 | |
B | GLN393 | |
B | ARG397 | |
A | TYR338 | |
A | PHE349 | |
A | ARG352 | |
A | LYS356 | |
A | TYR367 | |
A | GLN393 | |
A | ARG397 | |
B | GLY270 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950 |
Chain | Residue | Details |
A | HIS392 | |
B | HIS392 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07953 |
Chain | Residue | Details |
A | SER140 | |
B | SER140 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
A | HIS392 | |
A | HIS258 | |
A | GLU327 | |
A | ARG307 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
B | HIS392 | |
B | HIS258 | |
B | GLU327 | |
B | ARG307 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
A | ASN264 | |
A | HIS392 | |
A | ARG257 | |
A | HIS258 | |
A | ARG307 | |
A | GLU327 |
site_id | CSA4 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1qhf |
Chain | Residue | Details |
B | ASN264 | |
B | HIS392 | |
B | ARG257 | |
B | HIS258 | |
B | ARG307 | |
B | GLU327 |