2JFN
Crystal structure of Escherichia coli glutamate racemase in complex with L- Glutamate and activator UDP-MurNAc-ala
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008881 | molecular_function | glutamate racemase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GLU A1287 |
| Chain | Residue |
| A | ASP28 |
| A | CYS204 |
| A | THR205 |
| A | HIS206 |
| A | HOH2089 |
| A | SER29 |
| A | PHE58 |
| A | PRO59 |
| A | TYR60 |
| A | GLY61 |
| A | CYS92 |
| A | ASN93 |
| A | THR94 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE UMA A1286 |
| Chain | Residue |
| A | LEU100 |
| A | ARG104 |
| A | VAL112 |
| A | GLY113 |
| A | VAL114 |
| A | VAL115 |
| A | PRO116 |
| A | ALA117 |
| A | LYS119 |
| A | PRO120 |
| A | SER227 |
| A | ALA230 |
| A | ILE231 |
| A | ARG233 |
| A | ARG234 |
| A | HOH2084 |
| A | HOH2166 |
| A | HOH2213 |
| A | HOH2214 |
| A | HOH2215 |
| A | HOH2217 |
| A | HOH2218 |
| A | HOH2220 |
| A | HOH2221 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"O58403","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17568739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JFN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17568739","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JFN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| A | CYS204 | |
| A | ASP28 | |
| A | CYS92 | |
| A | SER29 |
