5W1Q
Crystal structure of alternate isoform of glutamate racemase from Helicobacter pylori bound to 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 A 301 |
| Chain | Residue |
| A | ASP7 |
| A | CYS181 |
| A | THR182 |
| A | HOH420 |
| A | HOH425 |
| A | HOH459 |
| A | SER8 |
| A | PRO38 |
| A | TYR39 |
| A | GLY40 |
| A | CYS70 |
| A | ASN71 |
| A | THR72 |
| A | THR116 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | ILE149 |
| A | GLU150 |
| A | ASN152 |
| A | TRP252 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | ILE153 |
| A | GLU155 |
| A | GLY156 |
| A | GLU157 |
| A | LEU158 |
| A | THR223 |
| A | HOH422 |
| B | TYR165 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue DGL B 301 |
| 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 | HOH409 |
| B | HOH434 |
| B | HOH449 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | ILE149 |
| B | GLU150 |
| B | ASN152 |
| B | LEU186 |
| B | TRP252 |
| B | HOH406 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | GLN103 |
| B | LEU207 |
| B | ILE208 |
| B | HIS209 |
| B | ALA213 |
| B | GLU216 |
| B | HOH408 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | GLU155 |
| B | GLY156 |
| B | GLU157 |
| B | LEU158 |
| B | LEU159 |
Functional Information from PROSITE/UniProt
