1ISU
THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0019646 | biological_process | aerobic electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0019646 | biological_process | aerobic electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 A 63 |
| Chain | Residue |
| A | CYS22 |
| A | CYS25 |
| A | GLN27 |
| A | PHE28 |
| A | CYS40 |
| A | CYS55 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 B 63 |
| Chain | Residue |
| B | CYS40 |
| B | CYS55 |
| B | CYS22 |
| B | CYS25 |
| B | PHE28 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:1453470 |
| Chain | Residue | Details |
| A | CYS22 | |
| A | CYS25 | |
| A | CYS40 | |
| A | CYS55 | |
| B | CYS22 | |
| B | CYS25 | |
| B | CYS40 | |
| B | CYS55 |
