1T75
Crystal structure of Escherichia coli beta carbonic anhydrase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015976 | biological_process | carbon utilization |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015976 | biological_process | carbon utilization |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| D | 0004089 | molecular_function | carbonate dehydratase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015976 | biological_process | carbon utilization |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051289 | biological_process | protein homotetramerization |
| E | 0004089 | molecular_function | carbonate dehydratase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0015976 | biological_process | carbon utilization |
| E | 0016829 | molecular_function | lyase activity |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 221 |
| Chain | Residue |
| A | CYS42 |
| A | ASP44 |
| A | HIS98 |
| A | CYS101 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 221 |
| Chain | Residue |
| B | CYS42 |
| B | ASP44 |
| B | HIS98 |
| B | CYS101 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 221 |
| Chain | Residue |
| D | ASP44 |
| D | HIS98 |
| D | CYS101 |
| D | CYS42 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 221 |
| Chain | Residue |
| E | CYS42 |
| E | ASP44 |
| E | HIS98 |
| E | CYS101 |
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. QYAVdvLevehIIIcGHygCG |
| Chain | Residue | Details |
| A | GLN82-GLY102 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11316870, ECO:0007744|PDB:1I6O, ECO:0007744|PDB:1I6P |
| Chain | Residue | Details |
| A | CYS42 | |
| D | ASP44 | |
| D | HIS98 | |
| D | CYS101 | |
| E | CYS42 | |
| E | ASP44 | |
| E | HIS98 | |
| E | CYS101 | |
| A | ASP44 | |
| A | HIS98 | |
| A | CYS101 | |
| B | CYS42 | |
| B | ASP44 | |
| B | HIS98 | |
| B | CYS101 | |
| D | 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 |
| D | ASP44 | |
| D | ARG46 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1i6p |
| Chain | Residue | Details |
| E | ASP44 | |
| E | ARG46 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 517 |
| Chain | Residue | Details |
| A | CYS42 | metal ligand |
| A | ASP44 | metal ligand, proton acceptor |
| A | ARG46 | electrostatic stabiliser, increase basicity |
| A | HIS98 | metal ligand |
| A | CYS101 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 517 |
| Chain | Residue | Details |
| B | CYS42 | metal ligand |
| B | ASP44 | metal ligand, proton acceptor |
| B | ARG46 | electrostatic stabiliser, increase basicity |
| B | HIS98 | metal ligand |
| B | CYS101 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 517 |
| Chain | Residue | Details |
| D | CYS42 | metal ligand |
| D | ASP44 | metal ligand, proton acceptor |
| D | ARG46 | electrostatic stabiliser, increase basicity |
| D | HIS98 | metal ligand |
| D | CYS101 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 517 |
| Chain | Residue | Details |
| E | CYS42 | metal ligand |
| E | ASP44 | metal ligand, proton acceptor |
| E | ARG46 | electrostatic stabiliser, increase basicity |
| E | HIS98 | metal ligand |
| E | CYS101 | metal ligand |
