3SID
Crystal structure of oxidized Symerythrin from Cyanophora paradoxa, azide adduct at 50% occupancy
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0009842 | cellular_component | cyanelle |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0009842 | cellular_component | cyanelle |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 200 |
| Chain | Residue |
| A | GLU71 |
| A | GLU128 |
| A | GLU162 |
| A | HIS165 |
| A | HOH183 |
| A | FE201 |
| A | AZI300 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FE A 201 |
| Chain | Residue |
| A | GLU71 |
| A | GLU131 |
| A | GLU162 |
| A | HOH183 |
| A | FE200 |
| A | HOH204 |
| A | AZI300 |
| A | GLU37 |
| A | GLU40 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZI A 300 |
| Chain | Residue |
| A | GLU40 |
| A | GLU71 |
| A | VAL127 |
| A | GLU128 |
| A | GLU131 |
| A | GLU162 |
| A | HOH183 |
| A | FE200 |
| A | FE201 |
| A | HOH204 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FE B 200 |
| Chain | Residue |
| B | GLU37 |
| B | GLU40 |
| B | GLU71 |
| B | GLU131 |
| B | GLU162 |
| B | HOH181 |
| B | HOH198 |
| B | FE201 |
| B | AZI300 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 201 |
| Chain | Residue |
| B | GLU71 |
| B | GLU128 |
| B | GLU162 |
| B | HIS165 |
| B | HOH181 |
| B | FE200 |
| B | AZI300 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AZI B 300 |
| Chain | Residue |
| B | GLU40 |
| B | GLU71 |
| B | VAL127 |
| B | GLU128 |
| B | GLU131 |
| B | GLU162 |
| B | HOH181 |
| B | HOH198 |
| B | FE200 |
| B | FE201 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 318 |
| Details | Domain: {"description":"Ferritin-like diiron","evidences":[{"source":"PROSITE-ProRule","id":"PRU00085","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21596985","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21872605","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QHB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QHC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SID","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21596985","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21872605","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QHC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SID","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"3-(L-phenylalan-2'-yl)-L-valine (Phe-Val)","evidences":[{"source":"PubMed","id":"21596985","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
