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 | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | V90302 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue V90 A 302 |
| Chain | Residue |
| A | HIS96 |
| A | HIS119 |
| A | LEU198 |
| A | THR199 |
| A | THR200 |
| A | ZN301 |
| A | HOH411 |
| A | HOH468 |
| A | ASN62 |
| A | HIS64 |
| A | GLN67 |
| A | GLN92 |
| A | HIS94 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | V90302 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue V90 B 302 |
| Chain | Residue |
| B | ASN62 |
| B | GLN67 |
| B | GLN92 |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | VAL121 |
| B | LEU198 |
| B | THR199 |
| B | THR200 |
| B | ZN301 |
| B | HOH426 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 301 |
| Chain | Residue |
| C | HIS94 |
| C | HIS96 |
| C | HIS119 |
| C | V90302 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue V90 C 302 |
| Chain | Residue |
| C | ASN62 |
| C | HIS64 |
| C | GLN67 |
| C | GLN92 |
| C | HIS94 |
| C | HIS96 |
| C | HIS119 |
| C | VAL121 |
| C | LEU198 |
| C | THR199 |
| C | THR200 |
| C | ZN301 |
| C | HOH1030 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 301 |
| Chain | Residue |
| D | HIS94 |
| D | HIS96 |
| D | HIS119 |
| D | V90302 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue V90 D 302 |
| Chain | Residue |
| D | ASN62 |
| D | HIS64 |
| D | GLN67 |
| D | GLN92 |
| D | HIS94 |
| D | HIS96 |
| D | HIS119 |
| D | LEU198 |
| D | THR199 |
| D | THR200 |
| D | ZN301 |
| D | HOH407 |
| D | HOH472 |
Functional Information from PROSITE/UniProt
| site_id | PS00162 |
| Number of Residues | 17 |
| Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVeghrFpaEIHVV |
| Chain | Residue | Details |
| A | SER105-VAL121 | |
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":"19805286","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 | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18703501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]} |
