Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 | 0005575 | cellular_component | cellular_component |
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 230 |
Chain | Residue |
A | CYS42 |
A | ASP44 |
A | HIS98 |
A | CYS101 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 231 |
Chain | Residue |
A | LEU121 |
A | ARG124 |
A | PHE128 |
B | ARG160 |
B | ARG198 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 232 |
Chain | Residue |
A | ARG160 |
A | LYS165 |
A | ARG198 |
B | LEU121 |
B | ARG124 |
B | PHE128 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 233 |
Chain | Residue |
A | PRO48 |
A | PRO48 |
A | ALA49 |
A | GLU50 |
A | GLU50 |
A | ARG64 |
A | ARG64 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 234 |
Chain | Residue |
A | SER45 |
A | ARG46 |
A | HIS98 |
A | THR99 |
A | PHE181 |
A | VAL183 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 230 |
Chain | Residue |
B | CYS42 |
B | ASP44 |
B | HIS98 |
B | CYS101 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 231 |
Chain | Residue |
B | PRO48 |
B | GLU50 |
B | GLU50 |
B | ARG64 |
B | ARG64 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 232 |
Chain | Residue |
B | SER45 |
B | ARG46 |
B | VAL47 |
B | HIS98 |
B | THR99 |
B | PHE181 |
B | VAL183 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 230 |
Chain | Residue |
C | CYS42 |
C | ASP44 |
C | HIS98 |
C | CYS101 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 231 |
Chain | Residue |
C | LEU121 |
C | ARG124 |
C | PHE128 |
D | ARG160 |
D | ARG198 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 232 |
Chain | Residue |
C | PRO48 |
C | GLU50 |
C | ARG64 |
C | HOH257 |
E | PRO48 |
E | ALA49 |
E | ARG64 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 C 233 |
Chain | Residue |
C | ASP44 |
C | SER45 |
C | ARG46 |
C | VAL47 |
C | HIS98 |
C | THR99 |
C | PHE181 |
C | VAL183 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 230 |
Chain | Residue |
D | CYS42 |
D | ASP44 |
D | HIS98 |
D | CYS101 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 231 |
Chain | Residue |
C | ARG160 |
C | ARG198 |
D | LEU121 |
D | ARG124 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 D 232 |
Chain | Residue |
D | SER45 |
D | ARG46 |
D | VAL47 |
D | HIS98 |
D | PHE181 |
D | VAL183 |
D | HOH240 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 230 |
Chain | Residue |
E | CYS42 |
E | ASP44 |
E | HIS98 |
E | CYS101 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 231 |
Chain | Residue |
E | LEU121 |
E | ARG124 |
F | ARG160 |
F | ARG198 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 232 |
Chain | Residue |
E | ARG160 |
E | LYS165 |
E | ARG198 |
F | LEU121 |
F | ARG124 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 233 |
Chain | Residue |
E | HIS98 |
E | PHE181 |
E | VAL183 |
E | SER45 |
E | ARG46 |
E | VAL47 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 230 |
Chain | Residue |
F | CYS42 |
F | ASP44 |
F | HIS98 |
F | CYS101 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 F 231 |
Chain | Residue |
D | PRO48 |
D | GLU50 |
D | ARG64 |
F | PRO48 |
F | ALA49 |
F | GLU50 |
F | ARG64 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 F 232 |
Chain | Residue |
F | SER45 |
F | ARG46 |
F | VAL47 |
F | HIS98 |
F | PHE181 |
F | VAL183 |
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
Chain | Residue | Details |
A | CYS42 | |
C | ASP44 | |
C | HIS98 | |
C | CYS101 | |
D | CYS42 | |
D | ASP44 | |
D | HIS98 | |
D | CYS101 | |
E | CYS42 | |
E | ASP44 | |
E | HIS98 | |
A | ASP44 | |
E | CYS101 | |
F | CYS42 | |
F | ASP44 | |
F | HIS98 | |
F | CYS101 | |
A | HIS98 | |
A | CYS101 | |
B | CYS42 | |
B | ASP44 | |
B | HIS98 | |
B | CYS101 | |
C | CYS42 | |
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 | |