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 | 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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS96 |
| B | HIS98 |
| B | HIS121 |
| B | V1F303 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG B 302 |
| Chain | Residue |
| B | LEU253 |
| B | LYS254 |
| B | ARG256 |
| A | LYS59 |
| A | ILE60 |
| A | ARG177 |
| B | ASP28 |
| B | GLN29 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE V1F B 303 |
| Chain | Residue |
| B | SER64 |
| B | HIS66 |
| B | ASN69 |
| B | GLN94 |
| B | HIS96 |
| B | HIS98 |
| B | HIS121 |
| B | VAL123 |
| B | PHE133 |
| B | ALA137 |
| B | LEU200 |
| B | THR201 |
| B | VAL202 |
| B | PRO204 |
| B | ZN301 |
| B | HOH608 |
| B | HOH637 |
| B | HOH639 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | GLY100 |
| B | SER101 |
| B | HIS105 |
| B | SER245 |
| B | HIS247 |
| B | HOH420 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | HIS96 |
| A | HIS98 |
| A | HIS121 |
| A | V1F303 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CIT A 302 |
| Chain | Residue |
| A | GLY100 |
| A | SER101 |
| A | HIS105 |
| A | SER245 |
| A | HIS247 |
| A | HOH485 |
| A | HOH618 |
| B | HOH499 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE V1F A 303 |
| Chain | Residue |
| A | HIS66 |
| A | ASN69 |
| A | GLN94 |
| A | HIS96 |
| A | HIS98 |
| A | HIS121 |
| A | VAL123 |
| A | PHE133 |
| A | VAL145 |
| A | LEU200 |
| A | THR201 |
| A | VAL202 |
| A | TRP211 |
| A | ZN301 |
| A | HOH487 |
| A | HOH590 |
| A | HOH641 |
| A | HOH643 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | GLN160 |
| A | GLN223 |
| A | LYS227 |
| A | HOH458 |
| A | HOH611 |
| A | HOH614 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | LEU166 |
| A | ASP167 |
| A | LYS170 |
| A | SER230 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 306 |
| Chain | Residue |
| A | ASP104 |
| A | VAL114 |
| A | SER115 |
| A | SER157 |
| A | HOH639 |
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 | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18618712","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
