4OMT
Crystal structure of human muscle phosphofructokinase (dissociated homodimer)
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 | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005945 | cellular_component | 6-phosphofructokinase complex |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008443 | molecular_function | phosphofructokinase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019900 | molecular_function | kinase binding |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| A | 0046716 | biological_process | muscle cell cellular homeostasis |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070061 | molecular_function | fructose binding |
| A | 0070095 | molecular_function | fructose-6-phosphate binding |
| A | 0097228 | cellular_component | sperm principal piece |
Functional Information from PROSITE/UniProt
| site_id | PS00433 |
| Number of Residues | 19 |
| Details | PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGtpsafDR |
| Chain | Residue | Details |
| A | ARG292-ARG310 | |
| A | ARG655-ARG673 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Region: {"description":"Interdomain linker"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47858","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47857","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29775581","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
