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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS226 |
| A | HIS228 |
| A | HIS251 |
| A | HOH606 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HIS140 |
| A | TRP141 |
| A | HIS200 |
| B | HIS244 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | HOH506 |
| A | HOH638 |
| A | HOH755 |
| A | GLN224 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | ARG151 |
| A | GLN326 |
| A | TYR327 |
| A | GLU328 |
| A | ILE341 |
| A | HOH512 |
| A | HOH538 |
| A | HOH595 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | ARG151 |
| A | VAL152 |
| A | GLU387 |
| A | HOH521 |
| A | HOH646 |
| B | GLY393 |
| B | VAL394 |
| B | ASP395 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | ARG159 |
| A | GLN338 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | GLU242 |
| A | HOH579 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue TRS A 408 |
| Chain | Residue |
| A | LEU373 |
| A | PHE375 |
| A | HOH575 |
| A | HOH611 |
| A | HOH675 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 409 |
| Chain | Residue |
| A | HIS244 |
| B | TRP141 |
| B | HIS200 |
| B | HOH671 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | HIS226 |
| B | HIS228 |
| B | HIS251 |
| B | HOH575 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | GLN224 |
| B | VAL253 |
| B | HOH586 |
| B | HOH602 |
| B | HOH611 |
| B | HOH683 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| B | PRO269 |
| B | GLY270 |
| B | GLU328 |
| B | HOH511 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| A | PRO208 |
| B | PHE160 |
| B | ARG384 |
| B | HOH514 |
| B | HOH547 |
| B | HOH707 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 405 |
| Chain | Residue |
| B | ARG159 |
| B | GLN338 |
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 | SER237-VAL253 | |
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":"19805286","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18703501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]} |
