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 | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Increases basicity of active site His"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
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 |
