3R2U
2.1 Angstrom Resolution Crystal Structure of Metallo-beta-lactamase from Staphylococcus aureus subsp. aureus COL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050313 | molecular_function | sulfur dioxygenase activity |
| A | 0070813 | biological_process | hydrogen sulfide metabolic process |
| B | 0006749 | biological_process | glutathione metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050313 | molecular_function | sulfur dioxygenase activity |
| B | 0070813 | biological_process | hydrogen sulfide metabolic process |
| C | 0006749 | biological_process | glutathione metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050313 | molecular_function | sulfur dioxygenase activity |
| C | 0070813 | biological_process | hydrogen sulfide metabolic process |
| D | 0006749 | biological_process | glutathione metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050313 | molecular_function | sulfur dioxygenase activity |
| D | 0070813 | biological_process | hydrogen sulfide metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 443 |
| Chain | Residue |
| A | HIS56 |
| A | HIS119 |
| A | ASP145 |
| A | HOH450 |
| A | HOH454 |
| A | HOH479 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 443 |
| Chain | Residue |
| B | HOH503 |
| B | HOH914 |
| B | HOH960 |
| B | HIS56 |
| B | HIS119 |
| B | ASP145 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 444 |
| Chain | Residue |
| B | HOH482 |
| B | HOH510 |
| B | HOH614 |
| B | HOH974 |
| B | HOH975 |
| B | HOH1057 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 445 |
| Chain | Residue |
| B | GLU314 |
| B | ASP338 |
| B | HOH1039 |
| B | HOH1040 |
| B | HOH1041 |
| D | ASN93 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 446 |
| Chain | Residue |
| B | ASP187 |
| B | HOH530 |
| B | HOH1057 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 443 |
| Chain | Residue |
| C | HIS56 |
| C | HIS119 |
| C | ASP145 |
| C | HOH522 |
| C | HOH540 |
| C | HOH972 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 444 |
| Chain | Residue |
| C | HIS94 |
| C | HOH473 |
| C | HOH554 |
| C | HOH976 |
| C | HOH977 |
| C | HOH978 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 445 |
| Chain | Residue |
| C | HIS288 |
| C | HOH559 |
| C | HOH1222 |
| C | HOH1223 |
| C | HOH1224 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 443 |
| Chain | Residue |
| D | HIS56 |
| D | HIS119 |
| D | ASP145 |
| D | HOH466 |
| D | HOH479 |
| D | HOH745 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 444 |
| Chain | Residue |
| D | HIS288 |
| D | GLU290 |
| D | HOH584 |
| D | HOH777 |
| D | HOH1030 |
| D | HOH1031 |
Functional Information from PROSITE/UniProt
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HGKLLETdLPF |
| Chain | Residue | Details |
| A | HIS388-PHE398 |
