3D47
Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg and D-malate
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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0009063 | biological_process | amino acid catabolic process |
| E | 0016052 | biological_process | carbohydrate catabolic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016836 | molecular_function | hydro-lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0009063 | biological_process | amino acid catabolic process |
| F | 0016052 | biological_process | carbohydrate catabolic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016836 | molecular_function | hydro-lyase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0009063 | biological_process | amino acid catabolic process |
| G | 0016052 | biological_process | carbohydrate catabolic process |
| G | 0016829 | molecular_function | lyase activity |
| G | 0016836 | molecular_function | hydro-lyase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0009063 | biological_process | amino acid catabolic process |
| H | 0016052 | biological_process | carbohydrate catabolic process |
| H | 0016829 | molecular_function | lyase activity |
| H | 0016836 | molecular_function | hydro-lyase activity |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0050032 | molecular_function | L-rhamnonate 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 | ASP226 |
| A | GLU252 |
| A | GLU280 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | ASP226 |
| B | GLU252 |
| B | GLU280 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 501 |
| Chain | Residue |
| C | ASP226 |
| C | GLU252 |
| C | GLU280 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 501 |
| Chain | Residue |
| D | ASP226 |
| D | GLU252 |
| D | GLU280 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 501 |
| Chain | Residue |
| E | ASP226 |
| E | GLU252 |
| E | GLU280 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 501 |
| Chain | Residue |
| F | ASP226 |
| F | GLU252 |
| F | GLU280 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG G 501 |
| Chain | Residue |
| G | ASP226 |
| G | GLU252 |
| G | GLU280 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG H 501 |
| Chain | Residue |
| H | ASP226 |
| H | GLU252 |
| H | GLU280 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLT A 502 |
| Chain | Residue |
| A | HIS33 |
| A | ARG59 |
| A | LYS189 |
| A | ASP226 |
| A | TRP228 |
| A | GLU252 |
| A | GLU280 |
| A | HIS329 |
| A | GLU349 |
| A | LEU351 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLT B 502 |
| Chain | Residue |
| B | HIS33 |
| B | ARG59 |
| B | LYS189 |
| B | ASP226 |
| B | TRP228 |
| B | GLU252 |
| B | GLU280 |
| B | HIS329 |
| B | GLU349 |
| B | LEU351 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLT C 502 |
| Chain | Residue |
| C | HIS33 |
| C | ARG59 |
| C | LYS189 |
| C | ASP226 |
| C | TRP228 |
| C | GLU252 |
| C | GLU280 |
| C | HIS329 |
| C | GLU349 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLT D 502 |
| Chain | Residue |
| D | HIS33 |
| D | ARG59 |
| D | LYS189 |
| D | ASP226 |
| D | TRP228 |
| D | GLU252 |
| D | GLU280 |
| D | HIS329 |
| D | GLU349 |
| D | LEU351 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLT E 502 |
| Chain | Residue |
| E | HIS33 |
| E | ARG59 |
| E | LYS189 |
| E | ASP226 |
| E | TRP228 |
| E | GLU252 |
| E | GLU280 |
| E | HIS329 |
| E | GLU349 |
| E | LEU351 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLT F 502 |
| Chain | Residue |
| F | HIS33 |
| F | ARG59 |
| F | LYS189 |
| F | ASP226 |
| F | TRP228 |
| F | GLU252 |
| F | GLU280 |
| F | HIS329 |
| F | GLU349 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MLT G 502 |
| Chain | Residue |
| G | HIS33 |
| G | ARG59 |
| G | LYS189 |
| G | ASP226 |
| G | TRP228 |
| G | GLU252 |
| G | GLU280 |
| G | HIS329 |
| G | GLU349 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLT H 502 |
| Chain | Residue |
| H | GLU349 |
| H | LEU351 |
| H | HIS33 |
| H | ARG59 |
| H | LYS189 |
| H | ASP226 |
| H | TRP228 |
| H | GLU252 |
| H | GLU280 |
| H | HIS329 |
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 | 8 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Site: {"description":"Increases basicity of active site His"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
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 |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 962 |
| Chain | Residue | Details |
| C | ASP226 | metal ligand |
| C | GLU252 | metal ligand |
| C | GLU280 | metal ligand |
| C | ASP302 | increase acidity, increase basicity, modifies pKa |
| C | HIS329 | proton acceptor, proton donor, proton relay |
| C | GLU349 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 962 |
| Chain | Residue | Details |
| D | ASP226 | metal ligand |
| D | GLU252 | metal ligand |
| D | GLU280 | metal ligand |
| D | ASP302 | increase acidity, increase basicity, modifies pKa |
| D | HIS329 | proton acceptor, proton donor, proton relay |
| D | GLU349 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 962 |
| Chain | Residue | Details |
| E | ASP226 | metal ligand |
| E | GLU252 | metal ligand |
| E | GLU280 | metal ligand |
| E | ASP302 | increase acidity, increase basicity, modifies pKa |
| E | HIS329 | proton acceptor, proton donor, proton relay |
| E | GLU349 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 962 |
| Chain | Residue | Details |
| F | ASP226 | metal ligand |
| F | GLU252 | metal ligand |
| F | GLU280 | metal ligand |
| F | ASP302 | increase acidity, increase basicity, modifies pKa |
| F | HIS329 | proton acceptor, proton donor, proton relay |
| F | GLU349 | electrostatic stabiliser |
| site_id | MCSA7 |
| Number of Residues | 6 |
| Details | M-CSA 962 |
| Chain | Residue | Details |
| G | ASP226 | metal ligand |
| G | GLU252 | metal ligand |
| G | GLU280 | metal ligand |
| G | ASP302 | increase acidity, increase basicity, modifies pKa |
| G | HIS329 | proton acceptor, proton donor, proton relay |
| G | GLU349 | electrostatic stabiliser |
| site_id | MCSA8 |
| Number of Residues | 6 |
| Details | M-CSA 962 |
| Chain | Residue | Details |
| H | ASP226 | metal ligand |
| H | GLU252 | metal ligand |
| H | GLU280 | metal ligand |
| H | ASP302 | increase acidity, increase basicity, modifies pKa |
| H | HIS329 | proton acceptor, proton donor, proton relay |
| H | GLU349 | electrostatic stabiliser |
