Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
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 | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
B | 0000287 | molecular_function | magnesium ion binding |
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 | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 3LR A 501 |
Chain | Residue |
A | HIS33 |
A | HIS329 |
A | GLU349 |
A | LEU351 |
A | TRP40 |
A | ILE45 |
A | ARG59 |
A | LYS189 |
A | ASP226 |
A | TRP228 |
A | GLU252 |
A | GLU280 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 500 |
Chain | Residue |
A | ASP226 |
A | GLU252 |
A | GLU280 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 500 |
Chain | Residue |
B | ASP226 |
B | GLU252 |
B | GLU280 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE 1N5 B 502 |
Chain | Residue |
B | HIS33 |
B | ILE45 |
B | ARG59 |
B | LYS189 |
B | PRO191 |
B | ASP226 |
B | TRP228 |
B | GLU252 |
B | GLU280 |
B | HIS329 |
B | GLU349 |
B | LEU351 |
Functional Information from PROSITE/UniProt
site_id | PS00908 |
Number of Residues | 26 |
Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. TiSCVDlALwDLfGKvvglPVykLLG |
Chain | Residue | Details |
A | THR136-GLY161 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS329 | |
B | HIS329 | |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS33 | |
B | GLU252 | |
B | GLU280 | |
B | GLU349 | |
A | ARG59 | |
A | ASP226 | |
A | GLU252 | |
A | GLU280 | |
A | GLU349 | |
B | HIS33 | |
B | ARG59 | |
B | ASP226 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Increases basicity of active site His |
Chain | Residue | Details |
A | ASP302 | |
B | ASP302 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | GLU349 | |
B | GLU349 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 962 |
Chain | Residue | Details |
A | ASP226 | metal ligand |
A | GLU252 | metal ligand |
A | GLU280 | metal ligand |
A | ASP302 | increase acidity, increase basicity, modifies pKa |
A | HIS329 | proton acceptor, proton donor, proton relay |
A | GLU349 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 962 |
Chain | Residue | Details |
B | ASP226 | metal ligand |
B | GLU252 | metal ligand |
B | GLU280 | metal ligand |
B | ASP302 | increase acidity, increase basicity, modifies pKa |
B | HIS329 | proton acceptor, proton donor, proton relay |
B | GLU349 | electrostatic stabiliser |