3CQD
Structure of the tetrameric inhibited form of phosphofructokinase-2 from Escherichia coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003872 | molecular_function | 6-phosphofructokinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008443 | molecular_function | phosphofructokinase activity |
| A | 0009024 | molecular_function | tagatose-6-phosphate kinase activity |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003872 | molecular_function | 6-phosphofructokinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008443 | molecular_function | phosphofructokinase activity |
| B | 0009024 | molecular_function | tagatose-6-phosphate kinase activity |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061615 | biological_process | glycolytic process through fructose-6-phosphate |
Functional Information from PDB Data
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP B 311 |
| Chain | Residue |
| A | LYS27 |
| B | ALA254 |
| B | GLY255 |
| B | MET258 |
| B | GLY283 |
| B | SER284 |
| B | THR287 |
| B | LYS185 |
| B | ASN187 |
| B | SER224 |
| B | LEU225 |
| B | GLY226 |
| B | PRO227 |
| B | GLY229 |
| B | SER248 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 313 |
| Chain | Residue |
| A | LYS185 |
| A | ASN187 |
| A | SER224 |
| A | LEU225 |
| A | GLY226 |
| A | PRO227 |
| A | GLY229 |
| A | SER248 |
| A | ALA254 |
| A | GLY255 |
| A | MET258 |
| A | GLY283 |
| A | SER284 |
| A | THR287 |
| B | LYS27 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ATP A 314 |
| Chain | Residue |
| A | TYR23 |
| A | PRO24 |
| A | GLY26 |
| A | LYS27 |
| B | ASN187 |
| B | LYS189 |
| B | GLY226 |
| B | PRO227 |
| B | THR251 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ATP B 312 |
| Chain | Residue |
| A | ASN187 |
| A | LYS189 |
| A | GLY226 |
| A | PRO227 |
| A | THR251 |
| B | TYR23 |
| B | PRO24 |
| B | GLY26 |
| B | LYS27 |
Functional Information from PROSITE/UniProt
| site_id | PS00583 |
| Number of Residues | 25 |
| Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGgGiNVAraIaHLGgsataifpaG |
| Chain | Residue | Details |
| A | GLY38-GLY62 |
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. STvGAGDsmvGAMT |
| Chain | Residue | Details |
| A | SER250-THR263 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23823238","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Structure of E. coli PFK2 in complex with substrates and products.","authors":["Pereira H.M.","Caniuguir A.","Baez M.","Cabrera R.","Garratt R.C.","Babul J."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Structure of E. coli PFK2 mutant Y23D.","authors":["Pereira H.M.","Caniuguir A.","Baez M.","Cabrera R.","Garratt R.C.","Babul J."]}},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23823238","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| A | ALA254 | |
| A | GLY255 | |
| A | GLY253 | |
| A | ASP256 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| B | ALA254 | |
| B | GLY255 | |
| B | GLY253 | |
| B | ASP256 |
