3CK5
Crystal structure of a racemase from Streptomyces coelicolor A3(2) with bound magnesium
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 | 0016836 | molecular_function | hydro-lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019388 | biological_process | galactose catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019388 | biological_process | galactose catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019388 | biological_process | galactose catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019388 | biological_process | galactose catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 400 |
| Chain | Residue |
| A | LYS166 |
| A | ASP197 |
| A | GLU223 |
| A | GLU249 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 400 |
| Chain | Residue |
| B | ASP197 |
| B | GLU223 |
| B | GLU249 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 400 |
| Chain | Residue |
| C | GLU223 |
| C | GLU249 |
| C | LYS166 |
| C | ASP197 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 400 |
| Chain | Residue |
| D | ASP197 |
| D | ASN199 |
| D | GLU223 |
| D | GLU249 |
Functional Information from PROSITE/UniProt
| site_id | PS00909 |
| Number of Residues | 32 |
| Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. LmvDaNmkwtvdgAiraaraLapfdlhwIEEP |
| Chain | Residue | Details |
| A | LEU194-PRO225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8ZL58","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q8ZL58","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of a racemase from Streptomyces coelicolor A3(2) with bound magnesium.","authors":["Rao K.N.","Burley S.K.","Swaminathan S."]}},{"source":"PDB","id":"3CK5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | ASP272 | |
| A | HIS299 | |
| A | LYS168 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| B | ASP272 | |
| B | HIS299 | |
| B | LYS168 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| C | ASP272 | |
| C | HIS299 | |
| C | LYS168 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| D | ASP272 | |
| D | HIS299 | |
| D | LYS168 |
