6TH5
Crystal structure of mature wildtype primitive Phytochelatin synthase from Nostoc spec. - Alr0975
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0010038 | biological_process | response to metal ion |
A | 0016740 | molecular_function | transferase activity |
A | 0016756 | molecular_function | glutathione gamma-glutamylcysteinyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0046938 | biological_process | phytochelatin biosynthetic process |
B | 0010038 | biological_process | response to metal ion |
B | 0016740 | molecular_function | transferase activity |
B | 0016756 | molecular_function | glutathione gamma-glutamylcysteinyltransferase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0046938 | biological_process | phytochelatin biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | ASP53 |
A | ASN159 |
A | GLN162 |
A | ASN165 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 302 |
Chain | Residue |
B | HOH478 |
A | GLU52 |
A | ASP163 |
A | HOH453 |
A | HOH471 |
B | HOH422 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CA B 301 |
Chain | Residue |
B | ASP53 |
B | ASN159 |
B | GLN162 |
B | ASN165 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CA B 302 |
Chain | Residue |
A | HOH447 |
A | HOH473 |
B | GLU52 |
B | ASP163 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CA B 303 |
Chain | Residue |
B | HOH403 |
B | HOH496 |
B | HOH497 |
B | HOH514 |