4IL0
Crystal structure of GlucDRP from E. coli K-12 MG1655 (EFI target EFI-506058)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008872 | molecular_function | glucarate dehydratase activity |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042838 | biological_process | D-glucarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008872 | molecular_function | glucarate dehydratase activity |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042838 | biological_process | D-glucarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008872 | molecular_function | glucarate dehydratase activity |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042838 | biological_process | D-glucarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008872 | molecular_function | glucarate dehydratase activity |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042838 | biological_process | D-glucarate catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0008872 | molecular_function | glucarate dehydratase activity |
| E | 0009063 | biological_process | amino acid catabolic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0042838 | biological_process | D-glucarate catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0008872 | molecular_function | glucarate dehydratase activity |
| F | 0009063 | biological_process | amino acid catabolic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0042838 | biological_process | D-glucarate catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0008872 | molecular_function | glucarate dehydratase activity |
| G | 0009063 | biological_process | amino acid catabolic process |
| G | 0016829 | molecular_function | lyase activity |
| G | 0042838 | biological_process | D-glucarate catabolic process |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0008872 | molecular_function | glucarate dehydratase activity |
| H | 0009063 | biological_process | amino acid catabolic process |
| H | 0016829 | molecular_function | lyase activity |
| H | 0042838 | biological_process | D-glucarate catabolic process |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT A 501 |
| Chain | Residue |
| A | ASN26 |
| A | HIS367 |
| A | ARG421 |
| A | ILE27 |
| A | HIS31 |
| A | TRP103 |
| A | PHE105 |
| A | LYS206 |
| A | ASN236 |
| A | HIS338 |
| A | ASN340 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT B 501 |
| Chain | Residue |
| B | ASN26 |
| B | HIS31 |
| B | TRP103 |
| B | PHE105 |
| B | PHE151 |
| B | LYS206 |
| B | ASN236 |
| B | HIS338 |
| B | ASN340 |
| B | HIS367 |
| B | ARG421 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT C 501 |
| Chain | Residue |
| C | ASN26 |
| C | ILE27 |
| C | HIS31 |
| C | TRP103 |
| C | PHE105 |
| C | LYS206 |
| C | ASN236 |
| C | HIS338 |
| C | ASN340 |
| C | HIS367 |
| C | ARG421 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CIT D 501 |
| Chain | Residue |
| D | ASN26 |
| D | ILE27 |
| D | HIS31 |
| D | PHE105 |
| D | PHE151 |
| D | LYS206 |
| D | ASN236 |
| D | HIS338 |
| D | ASN340 |
| D | HIS367 |
| D | ARG421 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CIT E 501 |
| Chain | Residue |
| E | ASN26 |
| E | HIS31 |
| E | LYS206 |
| E | ASN236 |
| E | HIS338 |
| E | ASN340 |
| E | HIS367 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL E 502 |
| Chain | Residue |
| E | GLY169 |
| E | ASN170 |
| E | HIS171 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT F 501 |
| Chain | Residue |
| F | ASN26 |
| F | ILE27 |
| F | HIS31 |
| F | TRP103 |
| F | PHE105 |
| F | PHE151 |
| F | LYS206 |
| F | ASN236 |
| F | HIS338 |
| F | ASN340 |
| F | HIS367 |
| F | ARG421 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CIT G 501 |
| Chain | Residue |
| G | ASN26 |
| G | ILE27 |
| G | HIS31 |
| G | PHE151 |
| G | LYS206 |
| G | ASN236 |
| G | HIS338 |
| G | ASN340 |
| G | HIS367 |
| G | ARG421 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL G 502 |
| Chain | Residue |
| G | ASN170 |
| G | HIS171 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CIT H 501 |
| Chain | Residue |
| H | ASN26 |
| H | ILE27 |
| H | HIS31 |
| H | TRP103 |
| H | PHE105 |
| H | PHE151 |
| H | LYS206 |
| H | ASN236 |
| H | HIS338 |
| H | ASN340 |
| H | HIS367 |
| H | ARG421 |
Functional Information from PROSITE/UniProt
| site_id | PS00908 |
| Number of Residues | 26 |
| Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AvAALEaALlDLlGKalnvPVceLLG |
| Chain | Residue | Details |
| A | ALA111-GLY136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 85 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






