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 |