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 CO A 230 |
Chain | Residue |
A | CYS42 |
A | ASP44 |
A | HIS98 |
A | CYS101 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO B 230 |
Chain | Residue |
B | CYS42 |
B | ASP44 |
B | HIS98 |
B | CYS101 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO C 230 |
Chain | Residue |
C | ASP44 |
C | HIS98 |
C | CYS101 |
C | CYS42 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO D 230 |
Chain | Residue |
D | CYS42 |
D | ASP44 |
D | HIS98 |
D | CYS101 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO E 230 |
Chain | Residue |
E | CYS42 |
E | ASP44 |
E | HIS98 |
E | CYS101 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CO F 230 |
Chain | Residue |
F | CYS42 |
F | ASP44 |
F | HIS98 |
F | CYS101 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ACT E 222 |
Chain | Residue |
C | THR73 |
C | ASP74 |
C | PHE75 |
D | ACT222 |
D | HOH238 |
E | THR73 |
E | ASP74 |
E | PHE75 |
E | ASN76 |
E | HOH246 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT D 222 |
Chain | Residue |
D | THR73 |
D | ASP74 |
D | PHE75 |
E | ACT222 |
E | HOH246 |
F | THR73 |
F | ASP74 |
F | PHE75 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACT B 222 |
Chain | Residue |
A | ACT222 |
A | ACT222 |
A | HOH250 |
A | HOH250 |
B | THR73 |
B | THR73 |
B | ASP74 |
B | ASP74 |
B | PHE75 |
B | PHE75 |
B | ASN76 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACT A 222 |
Chain | Residue |
A | THR73 |
A | THR73 |
A | ASP74 |
A | ASP74 |
A | PHE75 |
A | PHE75 |
A | HOH250 |
A | HOH250 |
B | ACT222 |
B | ACT222 |
B | HOH229 |
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 | |
A | ASP44 | |
E | HIS98 | |
E | CYS101 | |
F | CYS42 | |
F | ASP44 | |
F | HIS98 | |
F | CYS101 | |
A | HIS98 | |
A | CYS101 | |
B | CYS42 | |
B | ASP44 | |
B | HIS98 | |
B | CYS101 | |
C | CYS42 | |
C | ASP44 | |
C | HIS98 | |
C | CYS101 | |
D | CYS42 | |
D | ASP44 | |
D | HIS98 | |
D | CYS101 | |
E | CYS42 | |
E | ASP44 | |