Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0015976 | biological_process | carbon utilization |
A | 0016829 | molecular_function | lyase activity |
A | 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 | CYS51 |
A | ASP53 |
A | HIS104 |
A | CYS107 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 302 |
Chain | Residue |
A | HIS199 |
A | HOH303 |
A | HOH305 |
A | HOH307 |
A | HOH315 |
Functional Information from PROSITE/UniProt
site_id | PS00704 |
Number of Residues | 8 |
Details | PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CADSRVaA |
Chain | Residue | Details |
A | CYS51-ALA58 | |
site_id | PS00705 |
Number of Residues | 21 |
Details | PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. EYAVtvLnvplIVVlGHdsCG |
Chain | Residue | Details |
A | GLU88-GLY108 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | CYS51 | |
A | HIS104 | |
A | CYS107 | |
Chain | Residue | Details |
A | ASP53 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i6p |
Chain | Residue | Details |
A | ASP53 | |
A | ARG55 | |