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 | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
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 | 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