6L4C
Crystal structure of vicilin from Corylus avellana (Hazelnut)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004784 | molecular_function | superoxide dismutase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0034214 | biological_process | protein hexamerization |
| A | 0043245 | cellular_component | extraorganismal space |
| A | 0045735 | molecular_function | nutrient reservoir activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070207 | biological_process | protein homotrimerization |
| B | 0004784 | molecular_function | superoxide dismutase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0034214 | biological_process | protein hexamerization |
| B | 0043245 | cellular_component | extraorganismal space |
| B | 0045735 | molecular_function | nutrient reservoir activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070207 | biological_process | protein homotrimerization |
| C | 0004784 | molecular_function | superoxide dismutase activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0034214 | biological_process | protein hexamerization |
| C | 0043245 | cellular_component | extraorganismal space |
| C | 0045735 | molecular_function | nutrient reservoir activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070207 | biological_process | protein homotrimerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CU A 401 |
| Chain | Residue |
| A | TYR5 |
| A | CYS276 |
| A | PRO277 |
| A | HIS278 |
| A | HIS305 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CU B 401 |
| Chain | Residue |
| B | TYR5 |
| B | CYS276 |
| B | HIS278 |
| B | HIS305 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CU C 401 |
| Chain | Residue |
| C | TYR5 |
| C | CYS276 |
| C | PRO277 |
| C | HIS278 |
| C | HIS305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 408 |
| Details | Domain: {"description":"Cupin type-1 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 310 |
| Details | Domain: {"description":"Cupin type-1 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31753489","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6L4C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"15233621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15233621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
