4CNW
Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015670 | biological_process | carbon dioxide transport |
| A | 0016829 | molecular_function | lyase activity |
| A | 0018820 | molecular_function | cyanamide hydratase activity |
| A | 0038166 | biological_process | angiotensin-activated signaling pathway |
| A | 0044070 | biological_process | regulation of monoatomic anion transport |
| A | 0045177 | cellular_component | apical part of cell |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051453 | biological_process | regulation of intracellular pH |
| A | 2001150 | biological_process | positive regulation of dipeptide transmembrane transport |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015670 | biological_process | carbon dioxide transport |
| B | 0016829 | molecular_function | lyase activity |
| B | 0018820 | molecular_function | cyanamide hydratase activity |
| B | 0038166 | biological_process | angiotensin-activated signaling pathway |
| B | 0044070 | biological_process | regulation of monoatomic anion transport |
| B | 0045177 | cellular_component | apical part of cell |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051453 | biological_process | regulation of intracellular pH |
| B | 2001150 | biological_process | positive regulation of dipeptide transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 268 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | THR198 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 268 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | THR198 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 1001 |
| Chain | Residue |
| A | ASP174 |
| B | ASP34 |
| B | ASP36 |
| B | HOH2032 |
| B | HOH2035 |
| A | ASP57 |
Functional Information from PROSITE/UniProt
| site_id | PS00162 |
| Number of Residues | 17 |
| Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV |
| Chain | Residue | Details |
| A | SER105-VAL121 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15039588","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 256 |
| Details | Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
