Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| C | 0004089 | molecular_function | carbonate dehydratase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| D | 0004089 | molecular_function | carbonate dehydratase activity |
| D | 0008270 | molecular_function | zinc ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS91 |
| A | HIS93 |
| A | HIS117 |
| A | MKQ302 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue MKQ A 302 |
| Chain | Residue |
| A | HIS117 |
| A | VAL119 |
| A | LEU197 |
| A | THR198 |
| A | THR199 |
| A | ZN301 |
| A | ASN64 |
| A | HIS66 |
| A | GLN89 |
| A | HIS91 |
| A | HIS93 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS91 |
| B | HIS93 |
| B | HIS117 |
| B | MKQ302 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue MKQ B 302 |
| Chain | Residue |
| B | ASN64 |
| B | HIS66 |
| B | GLN89 |
| B | HIS91 |
| B | HIS93 |
| B | HIS117 |
| B | LEU197 |
| B | THR198 |
| B | THR199 |
| B | ZN301 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | PRO9 |
| B | ASP10 |
| B | SER14 |
| B | LYS17 |
| B | LYS18 |
| B | HOH436 |
| B | HOH460 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | THR44 |
| B | LEU46 |
| B | GLY80 |
| B | TYR190 |
| B | ARG192 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS91 |
| C | HIS93 |
| C | HIS117 |
| C | MKQ302 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue MKQ C 302 |
| Chain | Residue |
| C | ASN64 |
| C | HIS66 |
| C | GLN89 |
| C | HIS91 |
| C | HIS93 |
| C | HIS117 |
| C | ALA129 |
| C | LEU197 |
| C | THR198 |
| C | THR199 |
| C | ZN301 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS91 |
| D | HIS93 |
| D | HIS117 |
Functional Information from PROSITE/UniProt
| site_id | PS00162 |
| Number of Residues | 17 |
| Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVsgqhFaaELHIV |
| Chain | Residue | Details |
| A | SER103-VAL119 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11493685","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
