3CB3
Crystal structure of L-Talarate dehydratase from Polaromonas sp. JS666 complexed with Mg and L-glucarate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008867 | molecular_function | galactarate dehydratase activity |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990594 | molecular_function | L-altrarate dehydratase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008867 | molecular_function | galactarate dehydratase activity |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1990594 | molecular_function | L-altrarate dehydratase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0008867 | molecular_function | galactarate dehydratase activity |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1990594 | molecular_function | L-altrarate dehydratase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0008867 | molecular_function | galactarate dehydratase activity |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1990594 | molecular_function | L-altrarate dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | ASP211 |
| A | GLU237 |
| A | GLU263 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | ASP211 |
| B | GLU237 |
| B | GLU263 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 501 |
| Chain | Residue |
| C | ASP211 |
| C | GLU237 |
| C | GLU263 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 502 |
| Chain | Residue |
| D | ASP211 |
| D | GLU237 |
| D | GLU263 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | ALA252 |
| A | PHE255 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 503 |
| Chain | Residue |
| B | ALA252 |
| B | PHE255 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 502 |
| Chain | Residue |
| C | ALA252 |
| C | PHE255 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 503 |
| Chain | Residue |
| D | ALA252 |
| D | PHE255 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LGT A 601 |
| Chain | Residue |
| A | LYS67 |
| A | LYS180 |
| A | LYS182 |
| A | ASP211 |
| A | ASN213 |
| A | GLU237 |
| A | GLU263 |
| A | HIS313 |
| A | GLU333 |
| A | PHE335 |
| A | TRP337 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE LGT B 601 |
| Chain | Residue |
| B | LYS67 |
| B | LYS180 |
| B | LYS182 |
| B | ASP211 |
| B | ASN213 |
| B | GLU237 |
| B | GLU263 |
| B | HIS313 |
| B | GLU333 |
| B | PHE335 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LGT C 601 |
| Chain | Residue |
| C | LYS67 |
| C | LYS180 |
| C | LYS182 |
| C | ASP211 |
| C | ASN213 |
| C | GLU237 |
| C | GLU263 |
| C | HIS313 |
| C | GLU333 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LGT D 601 |
| Chain | Residue |
| D | LYS67 |
| D | LYS180 |
| D | LYS182 |
| D | ASP211 |
| D | ASN213 |
| D | GLU237 |
| D | GLU263 |
| D | HIS313 |
| D | GLU333 |
| D | PHE335 |
| D | TRP337 |
Functional Information from PROSITE/UniProt
| site_id | PS00909 |
| Number of Residues | 32 |
| Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LmvDaNqqwdrptAqrmcriFepfnlvwIEEP |
| Chain | Residue | Details |
| A | LEU208-PRO239 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | ASP286 | |
| A | HIS313 | |
| A | LYS182 | |
| A | GLU333 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| B | ASP286 | |
| B | HIS313 | |
| B | LYS182 | |
| B | GLU333 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| C | ASP286 | |
| C | HIS313 | |
| C | LYS182 | |
| C | GLU333 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| D | ASP286 | |
| D | HIS313 | |
| D | LYS182 | |
| D | GLU333 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | PRO340 | |
| A | LYS180 | |
| A | LYS182 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| B | PRO340 | |
| B | LYS180 | |
| B | LYS182 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| C | PRO340 | |
| C | LYS180 | |
| C | LYS182 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| D | PRO340 | |
| D | LYS180 | |
| D | LYS182 |
