Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015976 | biological_process | carbon utilization |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015976 | biological_process | carbon utilization |
| C | 0004089 | molecular_function | carbonate dehydratase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015976 | biological_process | carbon utilization |
| D | 0004089 | molecular_function | carbonate dehydratase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015976 | biological_process | carbon utilization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | CYS76 |
| A | HIS131 |
| A | CYS134 |
| A | BME303 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue BME A 302 |
| Chain | Residue |
| B | ZN301 |
| A | GLN67 |
| A | PHE116 |
| B | CYS76 |
| B | ASP78 |
| B | GLY135 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue BME A 303 |
| Chain | Residue |
| A | CYS76 |
| A | ASP78 |
| A | HIS131 |
| A | CYS134 |
| A | GLY135 |
| A | ZN301 |
| B | GLN67 |
| B | PHE116 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 304 |
| Chain | Residue |
| A | PHE116 |
| B | TRP138 |
| B | PGE302 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 305 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| A | BME302 |
| B | CYS76 |
| B | HIS131 |
| B | CYS134 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue PGE B 302 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | CYS76 |
| C | HIS131 |
| C | CYS134 |
| C | BME302 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue BME C 302 |
| Chain | Residue |
| C | GLY135 |
| C | ZN301 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | CYS76 |
| D | HIS131 |
| D | CYS134 |
| D | BME302 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue BME D 302 |
| Chain | Residue |
| D | ASP78 |
| D | GLY135 |
| D | ZN301 |
Functional Information from PROSITE/UniProt
| site_id | PS00705 |
| Number of Residues | 21 |
| Details | PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QFAIdvLkvkkIIVcGHtdCG |
| Chain | Residue | Details |
| A | GLN115-GLY135 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS76 | |
| D | CYS76 | |
| D | HIS131 | |
| D | CYS134 | |
| A | HIS131 | |
| A | CYS134 | |
| B | CYS76 | |
| B | HIS131 | |
| B | CYS134 | |
| C | CYS76 | |
| C | HIS131 | |
| C | CYS134 | |
