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 | 0009536 | cellular_component | plastid |
| 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 | 0009536 | cellular_component | plastid |
| 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 | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21596985, ECO:0000269|PubMed:21872605, ECO:0007744|PDB:3QHB, ECO:0007744|PDB:3QHC, ECO:0007744|PDB:3SID |
| Chain | Residue | Details |
| A | GLU37 | |
| A | GLU40 | |
| A | GLU131 | |
| B | GLU37 | |
| B | GLU40 | |
| B | GLU131 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21596985, ECO:0000269|PubMed:21872605, ECO:0007744|PDB:3QHC, ECO:0007744|PDB:3SID |
| Chain | Residue | Details |
| A | GLU71 | |
| A | GLU128 | |
| A | GLU162 | |
| A | HIS165 | |
| B | GLU71 | |
| B | GLU128 | |
| B | GLU162 | |
| B | HIS165 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CROSSLNK: 3-(L-phenylalan-2'-yl)-L-valine (Phe-Val) => ECO:0000269|PubMed:21596985 |
| Chain | Residue | Details |
| A | PHE17 | |
| A | VAL127 | |
| B | PHE17 | |
| B | VAL127 |
