3AV8
Refined Structure of Plant-type [2Fe-2S] Ferredoxin I from Aphanothece sacrum at 1.46 A 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 | 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 | 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 | 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 | 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 | 9 |
Details | BINDING SITE FOR RESIDUE FES A 98 |
Chain | Residue |
A | SER38 |
A | CYS39 |
A | ARG40 |
A | GLY42 |
A | ALA43 |
A | CYS44 |
A | CYS47 |
A | LEU76 |
A | CYS78 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 99 |
Chain | Residue |
B | LYS50 |
B | TYR74 |
B | LYS92 |
B | ALA95 |
B | HOH316 |
D | HOH124 |
D | HOH195 |
D | HOH280 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES B 98 |
Chain | Residue |
B | SER38 |
B | CYS39 |
B | ARG40 |
B | GLY42 |
B | ALA43 |
B | CYS44 |
B | CYS47 |
B | CYS78 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES C 98 |
Chain | Residue |
C | SER38 |
C | CYS39 |
C | ARG40 |
C | GLY42 |
C | ALA43 |
C | CYS44 |
C | CYS47 |
C | CYS78 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 99 |
Chain | Residue |
A | PRO55 |
A | GLY84 |
A | ASP85 |
A | HOH184 |
A | HOH268 |
C | ALA1 |
C | ASP20 |
C | HOH151 |
C | HOH263 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES D 98 |
Chain | Residue |
D | SER38 |
D | CYS39 |
D | ARG40 |
D | GLY42 |
D | ALA43 |
D | CYS44 |
D | CYS47 |
D | CYS78 |
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 | CYS39 | |
C | CYS44 | |
C | CYS47 | |
C | CYS78 | |
D | CYS39 | |
D | CYS44 | |
D | CYS47 | |
D | CYS78 | |
A | CYS44 | |
A | CYS47 | |
A | CYS78 | |
B | CYS39 | |
B | CYS44 | |
B | CYS47 | |
B | CYS78 | |
C | CYS39 |