2VVT
Glutamate Racemase (MurI) from E. faecalis in complex with a 9-Benzyl Purine inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0042802 | molecular_function | identical protein binding |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| A | 0071555 | biological_process | cell wall organization |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008881 | molecular_function | glutamate racemase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0047661 | molecular_function | amino-acid racemase activity |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE I24 A1269 |
| Chain | Residue |
| A | VAL14 |
| A | HOH2313 |
| A | HOH2314 |
| A | VAL152 |
| A | GLU153 |
| A | ASN155 |
| A | HIS187 |
| A | LEU190 |
| A | MET246 |
| A | ILE250 |
| A | HOH2194 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE I24 B1269 |
| Chain | Residue |
| A | ASN197 |
| A | GLY200 |
| A | SER201 |
| A | HIS202 |
| A | HOH2235 |
| B | VAL152 |
| B | GLU153 |
| B | ASN155 |
| B | GLU249 |
| B | ILE250 |
| B | HOH2355 |
| B | HOH2386 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL A1270 |
| Chain | Residue |
| A | ASP11 |
| A | SER12 |
| A | PRO42 |
| A | TYR43 |
| A | GLY44 |
| A | CYS74 |
| A | ASN75 |
| A | THR76 |
| A | THR118 |
| A | CYS185 |
| A | THR186 |
| A | HOH2021 |
| A | HOH2230 |
| A | HOH2315 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL B1270 |
| Chain | Residue |
| B | ASP11 |
| B | SER12 |
| B | PRO42 |
| B | TYR43 |
| B | GLY44 |
| B | CYS74 |
| B | ASN75 |
| B | THR76 |
| B | THR118 |
| B | CYS185 |
| B | THR186 |
| B | HIS187 |
| B | HOH2282 |
| B | HOH2388 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17568739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18614367","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JFO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JFP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VVT","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 | CYS185 | |
| A | CYS74 | |
| A | ASP11 | |
| A | SER12 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| B | CYS185 | |
| B | CYS74 | |
| B | ASP11 | |
| B | SER12 |
