2HIP
THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-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 | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 A 73 |
| Chain | Residue |
| A | CYS31 |
| A | CYS34 |
| A | PHE36 |
| A | CYS48 |
| A | CYS64 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SF4 B 73 |
| Chain | Residue |
| B | CYS31 |
| B | CYS34 |
| B | CYS48 |
| B | CYS64 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1917989","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7957187","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
