7BZ3
The mutant variant of PNGM-1. H257 was substituted for alanine to study substrate binding.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042780 | biological_process | tRNA 3'-end processing |
| A | 0042781 | molecular_function | 3'-tRNA processing endoribonuclease activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042780 | biological_process | tRNA 3'-end processing |
| B | 0042781 | molecular_function | 3'-tRNA processing endoribonuclease activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042780 | biological_process | tRNA 3'-end processing |
| C | 0042781 | molecular_function | 3'-tRNA processing endoribonuclease activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042780 | biological_process | tRNA 3'-end processing |
| D | 0042781 | molecular_function | 3'-tRNA processing endoribonuclease activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | ASP95 |
| A | HIS96 |
| A | ASP210 |
| A | HIS279 |
| A | ZN402 |
| A | HOH509 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | ASP210 |
| A | ZN401 |
| A | HOH509 |
| A | HIS91 |
| A | HIS93 |
| A | HIS188 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP95 |
| B | HIS96 |
| B | ASP210 |
| B | HIS279 |
| B | ZN402 |
| B | HOH513 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| B | HIS91 |
| B | HIS93 |
| B | HIS188 |
| B | ASP210 |
| B | ZN401 |
| B | HOH513 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 401 |
| Chain | Residue |
| C | ASP95 |
| C | HIS96 |
| C | ASP210 |
| C | HIS279 |
| C | ZN402 |
| C | HOH549 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 402 |
| Chain | Residue |
| C | HIS91 |
| C | HIS93 |
| C | HIS188 |
| C | ASP210 |
| C | ZN401 |
| C | HOH549 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 401 |
| Chain | Residue |
| D | ASP95 |
| D | HIS96 |
| D | ASP210 |
| D | HIS279 |
| D | ZN402 |
| D | HOH517 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 402 |
| Chain | Residue |
| D | HIS91 |
| D | HIS93 |
| D | HIS188 |
| D | ASP210 |
| D | ZN401 |
| D | HOH517 |
