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 | 0006730 | biological_process | one-carbon metabolic process |
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 | 0006730 | biological_process | one-carbon metabolic process |
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 B 301 |
Chain | Residue |
B | HIS96 |
B | HIS98 |
B | HIS121 |
B | ENN302 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue ENN B 302 |
Chain | Residue |
B | LEU200 |
B | THR201 |
B | VAL202 |
B | TRP211 |
B | ZN301 |
B | HOH465 |
B | HOH553 |
B | HOH698 |
B | GLN94 |
B | HIS96 |
B | HIS98 |
B | HIS121 |
B | VAL145 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | SER56 |
B | ASN180 |
B | HOH415 |
B | HOH538 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | LYS129 |
A | HOH518 |
B | ARG10 |
B | ALA241 |
B | PHE242 |
B | HOH462 |
B | HOH603 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | HIS96 |
A | HIS98 |
A | HIS121 |
A | ENN302 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue ENN A 302 |
Chain | Residue |
A | GLN94 |
A | HIS96 |
A | HIS98 |
A | HIS121 |
A | VAL145 |
A | LEU200 |
A | THR201 |
A | VAL202 |
A | TRP211 |
A | ZN301 |
A | HOH413 |
A | HOH475 |
A | HOH537 |
A | HOH615 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | ASN180 |
B | LYS52 |
B | ASP54 |
B | PRO55 |
B | HOH402 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue CIT A 304 |
Chain | Residue |
A | GLY100 |
A | SER101 |
A | HIS105 |
A | SER245 |
A | HIS247 |
A | HOH414 |
A | HOH415 |
A | HOH471 |
A | HOH538 |
A | HOH603 |
B | HOH536 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV |
Chain | Residue | Details |
B | SER107-VAL123 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | HIS66 | |
A | HIS66 | |
Chain | Residue | Details |
B | HIS96 | |
B | HIS98 | |
B | HIS121 | |
A | HIS96 | |
A | HIS98 | |
A | HIS121 | |
Chain | Residue | Details |
B | THR201 | |
A | THR201 | |