1DXF
2-dehydro-3-deoxy-galactarate aldolase from Escherichia coli in complex with pyruvate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008672 | molecular_function | 2-dehydro-3-deoxyglucarate aldolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0019394 | biological_process | glucarate catabolic process |
| A | 0042838 | biological_process | D-glucarate catabolic process |
| A | 0046392 | biological_process | galactarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008672 | molecular_function | 2-dehydro-3-deoxyglucarate aldolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0019394 | biological_process | glucarate catabolic process |
| B | 0042838 | biological_process | D-glucarate catabolic process |
| B | 0046392 | biological_process | galactarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 901 |
| Chain | Residue |
| A | GLU153 |
| A | ASP179 |
| A | PYR501 |
| A | HOH2027 |
| A | HOH2073 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 901 |
| Chain | Residue |
| B | HOH2079 |
| B | GLU153 |
| B | ASP179 |
| B | PYR501 |
| B | HOH2034 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR A 501 |
| Chain | Residue |
| A | ARG75 |
| A | GLN151 |
| A | GLU153 |
| A | GLY176 |
| A | PRO177 |
| A | SER178 |
| A | ASP179 |
| A | LEU216 |
| A | MG901 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR B 501 |
| Chain | Residue |
| B | ARG75 |
| B | GLN151 |
| B | GLU153 |
| B | PHE174 |
| B | GLY176 |
| B | PRO177 |
| B | SER178 |
| B | ASP179 |
| B | LEU216 |
| B | MG901 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS50 | |
| B | HIS50 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10921867 |
| Chain | Residue | Details |
| A | GLN151 | |
| A | GLU153 | |
| A | SER178 | |
| A | ASP179 | |
| B | GLN151 | |
| B | GLU153 | |
| B | SER178 | |
| B | ASP179 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG75 | |
| B | ARG75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Increases basicity of active site His => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP89 | |
| B | ASP89 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dxe |
| Chain | Residue | Details |
| A | ARG75 | |
| A | HIS50 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dxe |
| Chain | Residue | Details |
| B | ARG75 | |
| B | HIS50 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 846 |
| Chain | Residue | Details |
| A | HIS50 | proton acceptor, proton donor |
| A | ARG75 | electrostatic stabiliser |
| A | ASP89 | electrostatic stabiliser, modifies pKa |
| A | GLU153 | metal ligand |
| A | ASP179 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 846 |
| Chain | Residue | Details |
| B | HIS50 | proton acceptor, proton donor |
| B | ARG75 | electrostatic stabiliser |
| B | ASP89 | electrostatic stabiliser, modifies pKa |
| B | GLU153 | metal ligand |
| B | ASP179 | metal ligand |
