Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042597 | cellular_component | periplasmic space |
| 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 A 301 |
| Chain | Residue |
| A | HIS92 |
| A | HIS94 |
| A | HIS111 |
| A | AZI305 |
| A | HOH307 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AZI A 305 |
| Chain | Residue |
| A | THR177 |
| A | ZN301 |
| A | HOH307 |
| A | HOH308 |
| A | HOH365 |
| A | HIS92 |
| A | HIS94 |
| A | HIS111 |
| A | LEU176 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 302 |
| Chain | Residue |
| B | HIS92 |
| B | HIS94 |
| B | HIS111 |
| B | AZI306 |
| B | HOH309 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZI B 306 |
| Chain | Residue |
| B | HIS92 |
| B | HIS94 |
| B | HIS111 |
| B | LEU176 |
| B | THR177 |
| B | TRP187 |
| B | ZN302 |
| B | HOH309 |
| B | HOH310 |
| B | HOH464 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 311 |
| Chain | Residue |
| A | LYS132 |
| A | THR133 |
| A | ASN134 |
| A | GLY135 |
| A | ARG136 |
| A | HIS195 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 312 |
| Chain | Residue |
| B | ASN134 |
| B | GLY135 |
| B | ARG136 |
| B | HIS195 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 303 |
| Chain | Residue |
| A | HIS4 |
| A | ASN64 |
| A | HIS66 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 304 |
| Chain | Residue |
| B | HIS4 |
| B | ASN64 |
| B | HIS66 |
Functional Information from PROSITE/UniProt
| site_id | PS00162 |
| Number of Residues | 17 |
| Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SENqIkgrtFpmEAHFV |
| Chain | Residue | Details |
| A | SER97-VAL113 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 442 |
| 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 acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9761692","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ca2 |
| Chain | Residue | Details |
| A | THR177 | |
| A | HIS66 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ca2 |
| Chain | Residue | Details |
| B | THR177 | |
| B | HIS66 | |
