1K6M
Crystal Structure of Human Liver 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043540 | cellular_component | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex |
| A | 0045820 | biological_process | negative regulation of glycolytic process |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 1904539 | biological_process | negative regulation of glycolytic process through fructose-6-phosphate |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043540 | cellular_component | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex |
| B | 0045820 | biological_process | negative regulation of glycolytic process |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 1904539 | biological_process | negative 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 | 440 |
| Details | Region: {"description":"Fructose-2,6-bisphosphatase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"UniProtKB","id":"P07953","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P07953","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12379646","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q16875","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07953","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00950","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07953","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
