3OW5
Crystal structure of the Y200A mutant of gamma carbonic anhydrase from Methanosarcina thermophila
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0043199 | molecular_function | sulfate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0071890 | molecular_function | bicarbonate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 214 |
| Chain | Residue |
| A | HIS81 |
| A | HIS117 |
| A | HIS122 |
| A | HOH282 |
| A | BCT301 |
| A | SO4302 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 215 |
| Chain | Residue |
| A | HOH226 |
| A | HOH226 |
| A | HOH226 |
| A | MET55 |
| A | MET55 |
| A | MET55 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | GLU62 |
| A | GLN75 |
| A | HIS81 |
| A | HIS122 |
| A | VAL198 |
| A | ASN202 |
| A | ZN214 |
| A | HOH219 |
| A | HOH282 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT A 301 |
| Chain | Residue |
| A | GLU62 |
| A | GLN75 |
| A | HIS81 |
| A | ALA82 |
| A | LEU83 |
| A | HIS117 |
| A | HIS122 |
| A | ZN214 |
| A | HOH282 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10924115","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"10924115","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10924115","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10924115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8665839","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QRG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QRL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QRM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1THJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 516 |
| Chain | Residue | Details |
| A | GLU62 | electrostatic destabiliser, electrostatic stabiliser, proton acceptor, proton donor |
| A | GLN75 | electrostatic stabiliser |
| A | HIS81 | metal ligand |
| A | GLU84 | proton acceptor |
| A | HIS117 | metal ligand |
| A | HIS122 | metal ligand |
| A | ASN202 | electrostatic stabiliser, increase electrophilicity |
