1FXI
STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0022900 | biological_process | electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0022900 | biological_process | electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0022900 | biological_process | electron transport chain |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0022900 | biological_process | electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FES A 97 |
| Chain | Residue |
| A | TYR37 |
| A | CYS77 |
| A | SER38 |
| A | CYS39 |
| A | GLY42 |
| A | ALA43 |
| A | CYS44 |
| A | THR46 |
| A | CYS47 |
| A | LEU75 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES B 97 |
| Chain | Residue |
| B | SER38 |
| B | CYS39 |
| B | ARG40 |
| B | GLY42 |
| B | ALA43 |
| B | CYS44 |
| B | CYS47 |
| B | LEU75 |
| B | CYS77 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES C 97 |
| Chain | Residue |
| C | TYR37 |
| C | SER38 |
| C | CYS39 |
| C | ARG40 |
| C | GLY42 |
| C | ALA43 |
| C | CYS44 |
| C | CYS47 |
| C | CYS77 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FES D 97 |
| Chain | Residue |
| D | SER38 |
| D | CYS39 |
| D | ARG40 |
| D | GLY42 |
| D | ALA43 |
| D | CYS44 |
| D | THR46 |
| D | CYS47 |
| D | LEU75 |
| D | CYS77 |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACSTC |
| Chain | Residue | Details |
| A | CYS39-CYS47 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:2123937 |
| Chain | Residue | Details |
| A | ARG40 | |
| C | SER45 | |
| C | ALA48 | |
| C | VAL78 | |
| D | ARG40 | |
| D | SER45 | |
| D | ALA48 | |
| D | VAL78 | |
| A | SER45 | |
| A | ALA48 | |
| A | VAL78 | |
| B | ARG40 | |
| B | SER45 | |
| B | ALA48 | |
| B | VAL78 | |
| C | ARG40 |
