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 | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0043209 | cellular_component | myelin sheath |
| 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 | 0008270 | molecular_function | zinc ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS96 |
| B | HIS98 |
| B | HIS121 |
| B | THR201 |
| B | ACT305 |
| B | HOH424 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue CIT B 302 |
| Chain | Residue |
| B | GLU154 |
| B | SER245 |
| B | HIS247 |
| B | HOH466 |
| B | HOH506 |
| B | GLY100 |
| B | SER101 |
| B | HIS105 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue CIT B 303 |
| Chain | Residue |
| B | MET1 |
| B | ARG10 |
| B | GLU11 |
| B | HIS12 |
| B | ASN13 |
| B | HOH433 |
| B | HOH627 |
| B | HOH634 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PEG B 304 |
| Chain | Residue |
| A | LYS59 |
| A | ILE60 |
| A | ARG177 |
| B | ASP28 |
| B | GLN29 |
| B | LYS254 |
| B | ARG256 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ACT B 305 |
| Chain | Residue |
| B | HIS96 |
| B | HIS121 |
| B | VAL145 |
| B | LEU200 |
| B | THR201 |
| B | ZN301 |
| B | V90308 |
| B | HOH424 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| A | ILE60 |
| A | GLN175 |
| B | PRO197 |
| B | ARG256 |
| B | LYS257 |
| B | HOH454 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 307 |
| Chain | Residue |
| B | TYR116 |
| B | PRO217 |
| B | HOH406 |
| B | HOH409 |
| B | HOH447 |
| B | HOH467 |
| B | HOH520 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue V90 B 308 |
| Chain | Residue |
| B | ARG93 |
| B | GLN94 |
| B | HIS96 |
| B | VAL123 |
| B | PHE133 |
| B | HIS138 |
| B | VAL202 |
| B | ACT305 |
| B | HOH566 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS96 |
| A | HIS98 |
| A | HIS121 |
| A | THR201 |
| A | ACT307 |
| A | HOH417 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CIT A 302 |
| Chain | Residue |
| A | ARG10 |
| A | GLU11 |
| A | HIS12 |
| A | ASN13 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | LYS38 |
| A | GLN223 |
| A | LYS227 |
| A | HOH404 |
| A | HOH444 |
| A | HOH497 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ARG47 |
| A | PRO85 |
| A | HOH410 |
| A | HOH424 |
| A | HOH504 |
| A | HOH556 |
| A | HOH630 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue CIT A 305 |
| Chain | Residue |
| A | GLY100 |
| A | SER101 |
| A | HIS105 |
| A | SER245 |
| A | HIS247 |
| A | HOH435 |
| A | HOH498 |
| A | HOH551 |
| A | HOH622 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | LYS215 |
| A | GLN216 |
| A | PRO217 |
| A | HOH452 |
| A | HOH480 |
| A | HOH595 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue ACT A 307 |
| Chain | Residue |
| A | VAL145 |
| A | LEU200 |
| A | THR201 |
| A | ZN301 |
| A | V90308 |
| A | HOH417 |
| A | HIS96 |
| A | HIS121 |
| site_id | AD7 |
| Number of Residues | 14 |
| Details | binding site for residue V90 A 308 |
| Chain | Residue |
| A | ARG93 |
| A | GLN94 |
| A | HIS96 |
| A | VAL123 |
| A | PHE133 |
| A | HIS138 |
| A | VAL202 |
| A | LEU206 |
| A | ACT307 |
| A | HOH506 |
| A | HOH594 |
| A | HOH604 |
| A | HOH616 |
| B | LYS257 |
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 | SER107-VAL123 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 514 |
| Details | Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18618712","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
