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 | 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 | 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 | 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 |