2JFY
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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| B | 0042802 | molecular_function | identical protein binding |
| 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 | CYS181 |
| A | THR182 |
| A | HIS183 |
| A | HOH2094 |
| A | HOH2136 |
| A | SER8 |
| A | PRO38 |
| A | TYR39 |
| A | GLY40 |
| A | CYS70 |
| A | ASN71 |
| A | THR72 |
| A | THR116 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGL B1256 |
| Chain | Residue |
| B | ASP7 |
| B | SER8 |
| B | PRO38 |
| B | TYR39 |
| B | GLY40 |
| B | CYS70 |
| B | ASN71 |
| B | THR72 |
| B | THR116 |
| B | CYS181 |
| B | THR182 |
| B | HIS183 |
| B | HOH2098 |
| B | HOH2211 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:O58403, ECO:0000255|HAMAP-Rule:MF_00258 |
| Chain | Residue | Details |
| A | CYS70 | |
| A | CYS181 | |
| B | CYS70 | |
| B | CYS181 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:17568739, ECO:0000269|PubMed:19097892, ECO:0000269|PubMed:22877632, ECO:0007744|PDB:2JFX, ECO:0007744|PDB:2JFY, ECO:0007744|PDB:2JFZ, ECO:0007744|PDB:2W4I, ECO:0007744|PDB:4B1F |
| Chain | Residue | Details |
| A | ASP7 | |
| A | TYR39 | |
| A | ASN71 | |
| A | THR182 | |
| B | ASP7 | |
| B | TYR39 | |
| B | ASN71 | |
| B | THR182 |
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 |
