Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016829 | molecular_function | lyase activity |
A | 0043209 | cellular_component | myelin sheath |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0046872 | molecular_function | metal ion binding |
B | 0004089 | molecular_function | carbonate dehydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016829 | molecular_function | lyase activity |
B | 0043209 | cellular_component | myelin sheath |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0046872 | molecular_function | metal 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 | HIS96 |
A | HIS98 |
A | HIS121 |
A | WWX304 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | LYS161 |
A | ARG177 |
A | PHE178 |
A | THR179 |
A | HOH436 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | ASP112 |
A | GLY113 |
A | GLN160 |
A | GLN223 |
A | GLN224 |
A | HOH478 |
A | HOH491 |
A | HOH592 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE WWX A 304 |
Chain | Residue |
A | SER64 |
A | ASN69 |
A | GLN94 |
A | HIS96 |
A | HIS98 |
A | HIS121 |
A | PHE133 |
A | LEU200 |
A | THR201 |
A | VAL202 |
A | PRO204 |
A | ZN301 |
A | HOH553 |
A | HOH589 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | HIS96 |
B | HIS98 |
B | HIS121 |
B | WWX303 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | SER222 |
B | ALA226 |
B | HOH566 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE WWX B 303 |
Chain | Residue |
B | SER64 |
B | ASN69 |
B | GLN94 |
B | HIS96 |
B | HIS98 |
B | HIS121 |
B | VAL123 |
B | ALA137 |
B | LEU200 |
B | THR201 |
B | VAL202 |
B | ZN301 |
B | HOH447 |
B | HOH584 |
B | HOH616 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV |
Chain | Residue | Details |
A | SER107-VAL123 | |
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":"18618712","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |