5GK3
Native structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.8 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | GLN18 |
| A | PRO214 |
| A | SER258 |
| A | LEU259 |
| A | HOH515 |
| A | HOH559 |
| A | HOH584 |
| A | HOH614 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | GLU174 |
| A | HIS226 |
| A | HIS264 |
| A | HOH617 |
| A | HIS110 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PEG B 401 |
| Chain | Residue |
| A | SER88 |
| A | HIS91 |
| A | HIS92 |
| A | GLN95 |
| B | SER88 |
| B | HIS91 |
| B | HIS92 |
| B | GLN95 |
| B | HOH612 |
| B | HOH686 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | GLN18 |
| B | PRO214 |
| B | PHE216 |
| B | SER258 |
| B | LEU259 |
| B | HOH508 |
| B | HOH515 |
| B | HOH553 |
| B | HOH584 |
| B | HOH593 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | ILE87 |
| B | HIS91 |
| B | ALA125 |
| B | LYS128 |
| B | HIS129 |
| B | HOH613 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 404 |
| Chain | Residue |
| B | HIS110 |
| B | GLU174 |
| B | HIS226 |
| B | HIS264 |
| B | HOH635 |
Functional Information from PROSITE/UniProt
| site_id | PS00602 |
| Number of Residues | 12 |
| Details | ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC |
| Chain | Residue | Details |
| A | TYR100-CYS111 |
| site_id | PS00806 |
| Number of Residues | 12 |
| Details | ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE |
| Chain | Residue | Details |
| A | LEU171-GLU182 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10080900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10080900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8836102","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8939754","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 52 |
| Chain | Residue | Details |
| A | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS110 | metal ligand |
| A | HIS226 | metal ligand |
| A | HIS264 | metal ligand |
| A | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 52 |
| Chain | Residue | Details |
| B | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS110 | metal ligand |
| B | HIS226 | metal ligand |
| B | HIS264 | metal ligand |
| B | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
