3QHC
Crystal structure of Symerythrin from Cyanophora paradoxa, reduced with dithionite
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 | 9 |
Details | BINDING SITE FOR RESIDUE FE A 182 |
Chain | Residue |
A | GLU37 |
A | GLU40 |
A | GLU71 |
A | GLU131 |
A | GLU162 |
A | FE181 |
A | FE183 |
A | HOH204 |
A | HOH339 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE A 181 |
Chain | Residue |
A | GLU71 |
A | GLU128 |
A | GLU162 |
A | HIS165 |
A | FE182 |
A | HOH204 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE A 183 |
Chain | Residue |
A | GLU37 |
A | GLU71 |
A | HIS74 |
A | GLU162 |
A | FE182 |
A | HOH339 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FE B 182 |
Chain | Residue |
B | GLU37 |
B | GLU40 |
B | GLU71 |
B | GLU131 |
B | GLU162 |
B | FE181 |
B | FE183 |
B | HOH224 |
B | HOH293 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE B 183 |
Chain | Residue |
B | GLU37 |
B | GLU71 |
B | HIS74 |
B | GLU162 |
B | FE182 |
B | HOH293 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE B 181 |
Chain | Residue |
B | GLU71 |
B | GLU128 |
B | GLU162 |
B | HIS165 |
B | FE182 |
B | HOH224 |
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 |