Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0043209 | cellular_component | myelin sheath |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | THR199 |
| B | EWW302 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE EWW B 302 |
| Chain | Residue |
| B | HIS119 |
| B | VAL121 |
| B | PHE131 |
| B | VAL132 |
| B | VAL143 |
| B | SER197 |
| B | LEU198 |
| B | THR199 |
| B | VAL200 |
| B | PRO202 |
| B | VAL207 |
| B | TRP209 |
| B | ZN301 |
| B | HOH640 |
| B | HOH667 |
| B | ARG91 |
| B | GLN92 |
| B | HIS94 |
| B | HIS96 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 303 |
| Chain | Residue |
| A | ASP26 |
| A | GLN27 |
| A | LYS252 |
| A | ARG254 |
| B | LYS57 |
| B | ARG175 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DMS B 304 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CIT B 305 |
| Chain | Residue |
| A | ASP126 |
| A | HOH602 |
| B | GLY98 |
| B | SER99 |
| B | HIS103 |
| B | SER243 |
| B | HIS245 |
| B | HOH437 |
| B | HOH534 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG B 306 |
| Chain | Residue |
| A | THR73 |
| A | GLU74 |
| B | ASP101 |
| B | ASP102 |
| B | ILE150 |
| B | SER220 |
| B | HOH536 |
| B | HOH631 |
| B | HOH678 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 307 |
| Chain | Residue |
| A | ARG80 |
| B | PRO187 |
| B | SER188 |
| B | HOH603 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT B 308 |
| Chain | Residue |
| B | LYS36 |
| B | GLU37 |
| B | ASP110 |
| B | GLN158 |
| B | THR161 |
| B | ASP162 |
| B | GLN221 |
| B | GLN222 |
| B | LYS225 |
| B | HOH449 |
| B | HOH471 |
| B | HOH549 |
| B | HOH589 |
| B | HOH608 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 309 |
| Chain | Residue |
| B | ASN154 |
| B | SER155 |
| B | GLN156 |
| B | SER183 |
| B | HOH432 |
| B | HOH452 |
| B | HOH680 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | EWW302 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE EWW A 302 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | PHE131 |
| A | VAL132 |
| A | HIS136 |
| A | VAL143 |
| A | LEU198 |
| A | THR199 |
| A | VAL200 |
| A | TRP209 |
| A | ZN301 |
| A | HOH597 |
| A | HOH637 |
| A | HOH638 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI A 303 |
| Chain | Residue |
| A | SER99 |
| A | HIS103 |
| A | SER243 |
| A | HIS245 |
Functional Information from PROSITE/UniProt
| site_id | PS00162 |
| Number of Residues | 17 |
| Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV |
| Chain | Residue | Details |
| B | SER105-VAL121 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | HIS64 | |
| A | HIS64 | |
| Chain | Residue | Details |
| B | HIS94 | |
| B | HIS96 | |
| B | HIS119 | |
| A | HIS94 | |
| A | HIS96 | |
| A | HIS119 | |
| Chain | Residue | Details |
| B | THR199 | |
| A | THR199 | |
