2PP0
Crystal structure of L-talarate/galactarate dehydratase from Salmonella typhimurium LT2
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 | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 601 |
| Chain | Residue |
| A | ASP46 |
| A | LYS82 |
| A | LYS197 |
| A | ASN228 |
| A | GLU278 |
| A | HIS328 |
| A | HOH642 |
| A | HOH730 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 602 |
| Chain | Residue |
| B | LYS82 |
| B | PHE171 |
| B | LYS197 |
| B | ASN228 |
| B | GLU278 |
| B | HIS328 |
| B | ASP46 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 603 |
| Chain | Residue |
| C | ASP46 |
| C | LYS82 |
| C | LYS197 |
| C | ASN228 |
| C | GLU278 |
| C | HIS328 |
| C | HOH700 |
| C | HOH722 |
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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17649980","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17649980","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 27 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17649980","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Increases basicity of active site His"} |
| Chain | Residue | Details |
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 | LYS197 | |
| 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 | LYS197 | |
| 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 | LYS197 | |
| C | ASP301 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | LYS195 | |
| A | PRO355 | |
| A | LYS197 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| B | LYS195 | |
| B | PRO355 | |
| B | LYS197 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| C | LYS195 | |
| C | PRO355 | |
| C | LYS197 |
