2JFX
Crystal structure of Helicobacter pylori glutamate racemase in complex with D-Glutamate
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 | 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 | 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 | 14 |
| Details | BINDING SITE FOR RESIDUE DGL A1256 |
| Chain | Residue |
| A | ASP7 |
| A | THR116 |
| A | CYS181 |
| A | THR182 |
| A | HOH2029 |
| A | HOH2060 |
| A | SER8 |
| A | VAL37 |
| A | PRO38 |
| A | TYR39 |
| A | GLY40 |
| A | CYS70 |
| A | ASN71 |
| A | THR72 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL B1256 |
| Chain | Residue |
| B | ASP7 |
| B | SER8 |
| B | VAL37 |
| B | PRO38 |
| B | TYR39 |
| B | GLY40 |
| B | CYS70 |
| B | ASN71 |
| B | THR72 |
| B | THR116 |
| B | CYS181 |
| B | THR182 |
| B | HIS183 |
| B | HOH2047 |
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":"19097892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22877632","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W4I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4B1F","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 | CYS181 | |
| A | SER8 | |
| A | ASP7 | |
| A | CYS70 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1b73 |
| Chain | Residue | Details |
| B | CYS181 | |
| B | SER8 | |
| B | ASP7 | |
| B | CYS70 |
