3O8L
Structure of phosphofructokinase from rabbit skeletal muscle
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 | 0005737 | cellular_component | cytoplasm |
| A | 0005945 | cellular_component | 6-phosphofructokinase complex |
| A | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016208 | molecular_function | AMP binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048029 | molecular_function | monosaccharide binding |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070095 | molecular_function | fructose-6-phosphate binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005945 | cellular_component | 6-phosphofructokinase complex |
| B | 0006002 | biological_process | fructose 6-phosphate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016208 | molecular_function | AMP binding |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048029 | molecular_function | monosaccharide binding |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0070095 | molecular_function | fructose-6-phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP A 763 |
| Chain | Residue |
| A | SER23 |
| A | THR123 |
| A | GLY124 |
| A | GLY24 |
| A | TYR55 |
| A | ARG88 |
| A | CYS89 |
| A | LYS90 |
| A | GLY118 |
| A | GLY120 |
| A | SER121 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP A 764 |
| Chain | Residue |
| A | ASP173 |
| A | MET174 |
| A | TYR214 |
| A | PHE308 |
| A | ASN341 |
| A | SER377 |
| A | ASN381 |
| A | PHE538 |
| A | ASP543 |
| A | PHE671 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ATP A 765 |
| Chain | Residue |
| A | TRP227 |
| A | VAL228 |
| A | HIS242 |
| A | ARG246 |
| A | TYR385 |
| A | LYS386 |
| A | HIS390 |
| A | ILE391 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ATP B 763 |
| Chain | Residue |
| B | GLY24 |
| B | GLY25 |
| B | TYR55 |
| B | ARG88 |
| B | CYS89 |
| B | LYS90 |
| B | GLY118 |
| B | ASP119 |
| B | GLY120 |
| B | SER121 |
| B | THR123 |
| B | GLY124 |
| B | ASP166 |
| B | ASP168 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP B 764 |
| Chain | Residue |
| B | ASP173 |
| B | MET174 |
| B | TYR214 |
| B | PHE308 |
| B | ASN341 |
| B | SER377 |
| B | ASN381 |
| B | PHE538 |
| B | PHE671 |
| B | LYS678 |
| B | MET713 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ATP B 765 |
| Chain | Residue |
| B | ASP226 |
| B | VAL228 |
| B | HIS242 |
| B | ARG246 |
| B | TYR385 |
| B | LYS386 |
| B | ALA389 |
| B | HIS390 |
| B | ILE391 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 766 |
| Chain | Residue |
| A | ARG35 |
| A | ARG39 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 767 |
| Chain | Residue |
| A | ARG420 |
| A | ARG424 |
| A | GLY457 |
| A | GLY458 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 768 |
| Chain | Residue |
| A | ARG471 |
| A | THR528 |
| A | SER530 |
| A | ASN532 |
| A | ARG735 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 766 |
| Chain | Residue |
| B | ARG39 |
| B | SER74 |
| B | MET75 |
| B | GLY589 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 767 |
| Chain | Residue |
| B | GLY224 |
| B | ARG420 |
| B | ARG424 |
| B | GLY457 |
| B | GLY458 |
| B | THR460 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 768 |
| Chain | Residue |
| B | ARG471 |
| B | THR528 |
| B | SER530 |
| B | ASN532 |
| B | ARG735 |
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 | 20 |
| Details | Region: {"description":"Interdomain linker","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21241708","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| 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 | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47858","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47857","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P08237","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08237","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
