2ET7
Structural and spectroscopic insights into the mechanism of oxalate oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019430 | biological_process | removal of superoxide radicals |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048046 | cellular_component | apoplast |
| A | 0050162 | molecular_function | oxalate oxidase activity |
| A | 0071555 | biological_process | cell wall organization |
| A | 1902693 | cellular_component | superoxide dismutase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 202 |
| Chain | Residue |
| A | HIS88 |
| A | HIS90 |
| A | GLU95 |
| A | HIS137 |
| A | HOH203 |
Functional Information from PROSITE/UniProt
| site_id | PS00725 |
| Number of Residues | 14 |
| Details | GERMIN Germin family signature. GtnppHiHPrAtEI |
| Chain | Residue | Details |
| A | GLY83-ILE96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 151 |
| Details | Domain: {"description":"Cupin type-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2ET1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ETE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16291738","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ET1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ETE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11062559","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16291738","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ET1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ET7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ETE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16291738","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ETE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16291738","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ETE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1gqg |
| Chain | Residue | Details |
| A | GLU95 |
