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 |
