1EC7
E. COLI GLUCARATE DEHYDRATASE NATIVE ENZYME
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008872 | molecular_function | glucarate dehydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019394 | biological_process | glucarate catabolic process |
| A | 0042838 | biological_process | D-glucarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008872 | molecular_function | glucarate dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019394 | biological_process | glucarate catabolic process |
| B | 0042838 | biological_process | D-glucarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0008872 | molecular_function | glucarate dehydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019394 | biological_process | glucarate catabolic process |
| C | 0042838 | biological_process | D-glucarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0008872 | molecular_function | glucarate dehydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019394 | biological_process | glucarate catabolic process |
| D | 0042838 | biological_process | D-glucarate catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 498 |
| Chain | Residue |
| A | ASP235 |
| A | GLU260 |
| A | ASN289 |
| A | HOH1466 |
| A | HOH1488 |
| A | HOH1489 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 498 |
| Chain | Residue |
| B | HOH1365 |
| B | HOH1380 |
| B | HOH1762 |
| B | ASP235 |
| B | GLU260 |
| B | ASN289 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 498 |
| Chain | Residue |
| C | ASP235 |
| C | GLU260 |
| C | ASN289 |
| C | HOH1404 |
| C | HOH1572 |
| C | HOH1846 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 498 |
| Chain | Residue |
| D | ASP235 |
| D | GLU260 |
| D | ASN289 |
| D | HOH1447 |
| D | HOH1448 |
| D | HOH1869 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IPA C 601 |
| Chain | Residue |
| A | LEU302 |
| A | PHE332 |
| A | HOH2019 |
| C | GLY299 |
| C | SER303 |
| C | HOH1284 |
| C | HOH1354 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA D 602 |
| Chain | Residue |
| B | LEU302 |
| B | PHE332 |
| B | HOH1656 |
| D | GLY299 |
| D | SER303 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPA A 603 |
| Chain | Residue |
| A | GLY299 |
| A | SER303 |
| A | HOH1278 |
| C | LEU302 |
| C | PHE332 |
| C | HOH1831 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA D 604 |
| Chain | Residue |
| B | GLY299 |
| B | SER303 |
| D | LEU302 |
| D | PHE332 |
| D | HOH1204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 41 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS207 | |
| A | ASP313 | |
| A | HIS339 | |
| A | ASP366 | |
| A | LYS205 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS207 | |
| B | ASP313 | |
| B | HIS339 | |
| B | ASP366 | |
| B | LYS205 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS207 | |
| C | ASP313 | |
| C | HIS339 | |
| C | ASP366 | |
| C | LYS205 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS207 | |
| D | ASP313 | |
| D | HIS339 | |
| D | ASP366 | |
| D | LYS205 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS207 | |
| A | ASP366 | |
| A | LYS205 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS207 | |
| B | ASP366 | |
| B | LYS205 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS207 | |
| C | ASP366 | |
| C | LYS205 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS207 | |
| D | ASP366 | |
| D | LYS205 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| A | LYS205 | electrostatic stabiliser |
| A | LYS207 | electrostatic stabiliser |
| A | ASP235 | metal ligand |
| A | ASN237 | activator, electrostatic stabiliser |
| A | GLU260 | metal ligand |
| A | ASN289 | metal ligand |
| A | ASP313 | electrostatic stabiliser, modifies pKa |
| A | HIS339 | proton acceptor, proton donor |
| A | ASN341 | activator |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| B | LYS205 | electrostatic stabiliser |
| B | LYS207 | electrostatic stabiliser |
| B | ASP235 | metal ligand |
| B | ASN237 | activator, electrostatic stabiliser |
| B | GLU260 | metal ligand |
| B | ASN289 | metal ligand |
| B | ASP313 | electrostatic stabiliser, modifies pKa |
| B | HIS339 | proton acceptor, proton donor |
| B | ASN341 | activator |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| C | LYS205 | electrostatic stabiliser |
| C | LYS207 | electrostatic stabiliser |
| C | ASP235 | metal ligand |
| C | ASN237 | activator, electrostatic stabiliser |
| C | GLU260 | metal ligand |
| C | ASN289 | metal ligand |
| C | ASP313 | electrostatic stabiliser, modifies pKa |
| C | HIS339 | proton acceptor, proton donor |
| C | ASN341 | activator |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| D | LYS205 | electrostatic stabiliser |
| D | LYS207 | electrostatic stabiliser |
| D | ASP235 | metal ligand |
| D | ASN237 | activator, electrostatic stabiliser |
| D | GLU260 | metal ligand |
| D | ASN289 | metal ligand |
| D | ASP313 | electrostatic stabiliser, modifies pKa |
| D | HIS339 | proton acceptor, proton donor |
| D | ASN341 | activator |
