4OMT
Crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0005980 | biological_process | glycogen catabolic process |
| 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 | 0016208 | molecular_function | AMP binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0019900 | molecular_function | kinase binding |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0032024 | biological_process | positive regulation of insulin secretion |
| A | 0042593 | biological_process | glucose homeostasis |
| 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 | 0048029 | molecular_function | monosaccharide 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 | 0093001 | biological_process | glycolysis from storage polysaccharide through glucose-1-phosphate |
| 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 | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 |
| Chain | Residue | Details |
| A | ASP166 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03184 |
| Chain | Residue | Details |
| A | GLY25 | |
| A | ARG88 | |
| A | GLY118 | |
| A | ASP119 | |
| A | ARG201 | |
| A | ARG292 | |
| A | ARG566 | |
| A | ARG655 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03184 |
| Chain | Residue | Details |
| A | SER164 | |
| A | ARG735 | |
| A | MET208 | |
| A | GLU264 | |
| A | HIS298 | |
| A | ARG471 | |
| A | THR528 | |
| A | MET573 | |
| A | GLU629 | |
| A | HIS661 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylthreonine => ECO:0000250|UniProtKB:P00511 |
| Chain | Residue | Details |
| A | THR2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47858 |
| Chain | Residue | Details |
| A | SER133 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47857 |
| Chain | Residue | Details |
| A | SER377 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581 |
| Chain | Residue | Details |
| A | LYS557 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER667 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00511 |
| Chain | Residue | Details |
| A | SER775 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250 |
| Chain | Residue | Details |
| A | SER530 |
