Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0008270 | molecular_function | zinc ion binding |
A | 0015976 | biological_process | carbon utilization |
A | 0016829 | molecular_function | lyase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051289 | biological_process | protein homotetramerization |
B | 0004089 | molecular_function | carbonate dehydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0008270 | molecular_function | zinc ion binding |
B | 0015976 | biological_process | carbon utilization |
B | 0016829 | molecular_function | lyase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 300 |
Chain | Residue |
A | CYS42 |
A | ASP44 |
A | HIS98 |
A | CYS101 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BCT A 1498 |
Chain | Residue |
A | ARG64 |
A | TYR181 |
A | HOH1499 |
A | HOH1500 |
A | TRP39 |
A | VAL47 |
A | PRO48 |
A | ALA49 |
A | LEU52 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 300 |
Chain | Residue |
B | CYS42 |
B | ASP44 |
B | HIS98 |
B | CYS101 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BCT B 2498 |
Chain | Residue |
B | TRP39 |
B | GLY41 |
B | VAL47 |
B | ALA49 |
B | ARG64 |
B | TYR181 |
B | HOH2499 |
B | HOH2500 |
Functional Information from PROSITE/UniProt
site_id | PS00704 |
Number of Residues | 8 |
Details | PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVpA |
Chain | Residue | Details |
A | CYS42-ALA49 | |
site_id | PS00705 |
Number of Residues | 21 |
Details | PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLevehIIIcGHygCG |
Chain | Residue | Details |
A | GLN82-GLY102 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | CYS42 | |
A | ASP44 | |
A | HIS98 | |
A | CYS101 | |
B | CYS42 | |
B | ASP44 | |
B | HIS98 | |
B | CYS101 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i6p |
Chain | Residue | Details |
A | ASP44 | |
A | ARG46 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i6p |
Chain | Residue | Details |
B | ASP44 | |
B | ARG46 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 517 |
Chain | Residue | Details |
A | CYS42 | metal ligand |
A | ASP44 | metal ligand, proton acceptor |
A | ARG46 | electrostatic stabiliser, increase basicity |
A | HIS98 | metal ligand |
A | CYS101 | metal ligand |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 517 |
Chain | Residue | Details |
B | CYS42 | metal ligand |
B | ASP44 | metal ligand, proton acceptor |
B | ARG46 | electrostatic stabiliser, increase basicity |
B | HIS98 | metal ligand |
B | CYS101 | metal ligand |