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 |
B | 0004089 | molecular_function | carbonate dehydratase activity |
B | 0005515 | molecular_function | protein binding |
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 | 0005515 | molecular_function | protein binding |
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 | 0005515 | molecular_function | protein binding |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SCN A 501 |
Chain | Residue |
A | CYS51 |
A | ASP53 |
A | HIS104 |
A | CYS107 |
A | GLY108 |
A | ZN401 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | SCN501 |
A | CYS51 |
A | HIS104 |
A | CYS107 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN A 405 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN A 409 |
Chain | Residue |
A | HIS158 |
A | ASP198 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN A 400 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SCN B 502 |
Chain | Residue |
A | TYR89 |
B | ASP53 |
B | HIS104 |
B | CYS107 |
B | GLY108 |
B | ZN402 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | CYS51 |
B | HIS104 |
B | CYS107 |
B | SCN502 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN B 408 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SCN C 503 |
Chain | Residue |
C | CYS51 |
C | ASP53 |
C | HIS104 |
C | CYS107 |
C | GLY108 |
C | ZN403 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SCN C 504 |
Chain | Residue |
C | GLN42 |
D | ASP53 |
D | ALA75 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 403 |
Chain | Residue |
C | CYS51 |
C | HIS104 |
C | CYS107 |
C | SCN503 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 404 |
Chain | Residue |
D | CYS51 |
D | HIS104 |
D | CYS107 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN D 406 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN D 407 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN D 410 |
Chain | Residue |
D | HIS158 |
D | ASP198 |
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 | |
D | CYS51 | |
D | HIS104 | |
D | CYS107 | |
A | HIS104 | |
A | CYS107 | |
B | CYS51 | |
B | HIS104 | |
B | CYS107 | |
C | CYS51 | |
C | HIS104 | |
C | CYS107 | |
Chain | Residue | Details |
A | ASP53 | |
B | ASP53 | |
C | ASP53 | |
D | 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 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i6p |
Chain | Residue | Details |
B | ASP53 | |
B | ARG55 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i6p |
Chain | Residue | Details |
C | ASP53 | |
C | ARG55 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i6p |
Chain | Residue | Details |
D | ASP53 | |
D | ARG55 | |