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 | E1G302 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE E1G A 302 |
| Chain | Residue |
| A | SER133 |
| A | LEU197 |
| A | THR198 |
| A | THR199 |
| A | PRO201 |
| A | ZN301 |
| A | GLN89 |
| A | HIS91 |
| A | HIS93 |
| A | HIS117 |
| A | VAL119 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 303 |
| Chain | Residue |
| A | PHE151 |
| A | HOH584 |
| C | LYS18 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | HIS91 |
| B | HIS93 |
| B | HIS117 |
| B | E1G302 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE E1G B 302 |
| Chain | Residue |
| B | GLN89 |
| B | HIS91 |
| B | HIS93 |
| B | HIS117 |
| B | VAL119 |
| B | SER133 |
| B | LEU197 |
| B | THR198 |
| B | THR199 |
| B | PRO201 |
| B | TRP208 |
| B | ZN301 |
| B | HOH580 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 303 |
| Chain | Residue |
| B | TRP4 |
| B | ASN64 |
| B | HIS66 |
| B | GLN89 |
| B | HIS91 |
| B | THR199 |
| B | HOH566 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | ASP156 |
| B | SER160 |
| B | HOH513 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | HIS91 |
| C | HIS93 |
| C | HIS117 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | HIS91 |
| D | HIS93 |
| D | HIS117 |
| D | E1G302 |
| site_id | BC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE E1G D 302 |
| Chain | Residue |
| D | GLN89 |
| D | HIS91 |
| D | HIS93 |
| D | HIS117 |
| D | VAL119 |
| D | SER133 |
| D | LEU197 |
| D | THR198 |
| D | THR199 |
| D | PRO201 |
| D | ZN301 |
| D | PEG303 |
| D | HOH535 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG D 303 |
| Chain | Residue |
| D | TRP4 |
| D | ASN64 |
| D | HIS66 |
| D | SER67 |
| D | GLN89 |
| D | HIS91 |
| D | THR199 |
| D | E1G302 |
| D | HOH422 |
| D | HOH533 |
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"}]} |
4KP8
