Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| 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 |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015976 | biological_process | carbon utilization |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004089 | molecular_function | carbonate dehydratase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015976 | biological_process | carbon utilization |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004089 | molecular_function | carbonate dehydratase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015976 | biological_process | carbon utilization |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004089 | molecular_function | carbonate dehydratase activity |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0015976 | biological_process | carbon utilization |
| E | 0016829 | molecular_function | lyase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0004089 | molecular_function | carbonate dehydratase activity |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0015976 | biological_process | carbon utilization |
| F | 0016829 | molecular_function | lyase activity |
| F | 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 1230 |
| Chain | Residue |
| A | CYS42 |
| A | ASP44 |
| A | HIS98 |
| A | CYS101 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2230 |
| Chain | Residue |
| B | CYS42 |
| B | ASP44 |
| B | HIS98 |
| B | CYS101 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 3230 |
| Chain | Residue |
| C | ASP44 |
| C | HIS98 |
| C | CYS101 |
| C | CYS42 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 4230 |
| Chain | Residue |
| D | CYS42 |
| D | ASP44 |
| D | HIS98 |
| D | CYS101 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 5230 |
| Chain | Residue |
| E | CYS42 |
| E | ASP44 |
| E | HIS98 |
| E | CYS101 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 6230 |
| Chain | Residue |
| F | CYS42 |
| F | ASP44 |
| F | HIS98 |
| F | CYS101 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1001 |
| Chain | Residue |
| A | LEU121 |
| A | ARG124 |
| B | ARG160 |
| B | LYS165 |
| B | ARG198 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1002 |
| Chain | Residue |
| A | ARG160 |
| A | LYS165 |
| A | ARG198 |
| B | LEU121 |
| B | ARG124 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1003 |
| Chain | Residue |
| C | LEU121 |
| C | ARG124 |
| D | ARG160 |
| D | ARG198 |
| D | HOH4259 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1004 |
| Chain | Residue |
| C | ARG160 |
| C | ARG198 |
| D | ARG124 |
| D | HOH4260 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1005 |
| Chain | Residue |
| E | ARG124 |
| E | PHE128 |
| E | HOH5242 |
| F | ARG160 |
| F | ARG198 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1006 |
| Chain | Residue |
| E | ARG160 |
| E | ARG198 |
| E | HOH5239 |
| E | HOH5243 |
| F | ARG124 |
| F | PHE128 |
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. QYAVdvLkiehIIIcGHtnCG |
| Chain | Residue | Details |
| A | GLN82-GLY102 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16584170","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A8D","evidenceCode":"ECO:0007744"}]} |
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 | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| C | ASP44 | |
| C | ARG46 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| D | ASP44 | |
| D | ARG46 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| E | ASP44 | |
| E | ARG46 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| F | ASP44 | |
| F | ARG46 | |
