2PP3
Crystal structure of L-talarate/galactarate dehydratase mutant K197A liganded 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 | 0046392 | biological_process | galactarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903663 | biological_process | L-altrarate catabolic process |
| 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 | 0046392 | biological_process | galactarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1903663 | biological_process | L-altrarate catabolic process |
| 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 | 0046392 | biological_process | galactarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1903663 | biological_process | L-altrarate catabolic process |
| C | 1990594 | molecular_function | L-altrarate dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 901 |
| Chain | Residue |
| A | ASP226 |
| A | GLU252 |
| A | GLU278 |
| A | LGT501 |
| A | HOH1053 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 902 |
| Chain | Residue |
| B | HOH980 |
| B | ASP226 |
| B | GLU252 |
| B | GLU278 |
| B | LGT502 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 903 |
| Chain | Residue |
| C | LYS195 |
| C | ASP226 |
| C | GLU252 |
| C | GLU278 |
| C | LGT503 |
| C | HOH976 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE LGT A 501 |
| Chain | Residue |
| A | ASP46 |
| A | LYS48 |
| A | LYS82 |
| A | ARG83 |
| A | THR167 |
| A | PHE171 |
| A | LYS195 |
| A | ASP226 |
| A | ASN228 |
| A | GLU252 |
| A | GLU278 |
| A | HIS328 |
| A | GLU348 |
| A | PHE350 |
| A | TRP352 |
| A | MG901 |
| A | HOH915 |
| A | HOH1050 |
| A | HOH1051 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE LGT B 502 |
| Chain | Residue |
| B | VAL44 |
| B | ASP46 |
| B | LYS48 |
| B | LYS82 |
| B | ARG83 |
| B | THR167 |
| B | LYS195 |
| B | ASP226 |
| B | ASN228 |
| B | GLU252 |
| B | GLU278 |
| B | HIS328 |
| B | GLU348 |
| B | PHE350 |
| B | TRP352 |
| B | MG902 |
| B | HOH926 |
| B | HOH977 |
| B | HOH978 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE LGT C 503 |
| Chain | Residue |
| C | VAL44 |
| C | ASP46 |
| C | LYS48 |
| C | LYS82 |
| C | ARG83 |
| C | LYS195 |
| C | ASP226 |
| C | ASN228 |
| C | GLU252 |
| C | GLU278 |
| C | HIS328 |
| C | GLU348 |
| C | PHE350 |
| C | TRP352 |
| C | MG903 |
| C | HOH949 |
| C | HOH972 |
| C | HOH973 |
Functional Information from PROSITE/UniProt
| site_id | PS00909 |
| Number of Residues | 32 |
| Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LmvDaNqqwdretAirmgrkMeqfnliwIEEP |
| Chain | Residue | Details |
| A | LEU223-PRO254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:17649980 |
| Chain | Residue | Details |
| A | ALA197 | |
| B | ALA197 | |
| C | ALA197 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17649980 |
| Chain | Residue | Details |
| A | HIS328 | |
| B | HIS328 | |
| C | HIS328 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17649980 |
| Chain | Residue | Details |
| A | ASP46 | |
| B | LYS82 | |
| B | LYS195 | |
| B | ASP226 | |
| B | ASN228 | |
| B | GLU252 | |
| B | GLU278 | |
| B | GLU348 | |
| C | ASP46 | |
| C | LYS82 | |
| C | LYS195 | |
| A | LYS82 | |
| C | ASP226 | |
| C | ASN228 | |
| C | GLU252 | |
| C | GLU278 | |
| C | GLU348 | |
| A | LYS195 | |
| A | ASP226 | |
| A | ASN228 | |
| A | GLU252 | |
| A | GLU278 | |
| A | GLU348 | |
| B | ASP46 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | SITE: Increases basicity of active site His |
| Chain | Residue | Details |
| A | ASP301 | |
| B | ASP301 | |
| C | ASP301 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | HIS328 | |
| A | GLU348 | |
| A | ALA197 | |
| A | ASP301 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| B | HIS328 | |
| B | GLU348 | |
| B | ALA197 | |
| B | ASP301 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| C | HIS328 | |
| C | GLU348 | |
| C | ALA197 | |
| C | ASP301 |
