Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009579 | cellular_component | thylakoid |
A | 0015979 | biological_process | photosynthesis |
A | 0016020 | cellular_component | membrane |
B | 0046872 | molecular_function | metal ion binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0015979 | biological_process | photosynthesis |
E | 0015979 | biological_process | photosynthesis |
E | 0042314 | molecular_function | bacteriochlorophyll binding |
E | 0046872 | molecular_function | metal ion binding |
F | 0015979 | biological_process | photosynthesis |
F | 0042314 | molecular_function | bacteriochlorophyll binding |
F | 0046872 | molecular_function | metal ion binding |
G | 0015979 | biological_process | photosynthesis |
G | 0042314 | molecular_function | bacteriochlorophyll binding |
G | 0046872 | molecular_function | metal ion binding |
a | 0009579 | cellular_component | thylakoid |
a | 0015979 | biological_process | photosynthesis |
a | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00198 |
Number of Residues | 12 |
Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CvGCGlCLdKCP |
Chain | Residue | Details |
B | CYS140-PRO151 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
E | HIS111 | |
F | HIS298 | |
G | HIS111 | |
G | HIS146 | |
G | HIS290 | |
G | HIS297 | |
G | HIS298 | |
E | HIS146 | |
E | HIS290 | |
E | HIS297 | |
E | HIS298 | |
F | HIS111 | |
F | HIS146 | |
F | HIS290 | |
F | HIS297 | |