3W5U
Cross-linked complex between Ferredoxin and Ferredoxin-NADP+ reductase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
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 | 0016491 | molecular_function | oxidoreductase activity |
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 |
E | 0016491 | molecular_function | oxidoreductase activity |
F | 0009055 | molecular_function | electron transfer activity |
F | 0022900 | biological_process | electron transport chain |
F | 0051536 | molecular_function | iron-sulfur cluster binding |
F | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
G | 0016491 | molecular_function | oxidoreductase activity |
H | 0009055 | molecular_function | electron transfer activity |
H | 0022900 | biological_process | electron transport chain |
H | 0051536 | molecular_function | iron-sulfur cluster binding |
H | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE FAD A 401 |
Chain | Residue |
A | ARG93 |
A | GLY130 |
A | VAL131 |
A | CYS132 |
A | SER133 |
A | THR172 |
A | GLU312 |
A | TYR314 |
D | SER38 |
A | LEU94 |
A | TYR95 |
A | SER96 |
A | CYS114 |
A | VAL115 |
A | LYS116 |
A | LEU118 |
A | TYR120 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES B 101 |
Chain | Residue |
B | SER38 |
B | CYS39 |
B | ARG40 |
B | GLY42 |
B | SER43 |
B | CYS44 |
B | CYS47 |
B | LEU75 |
B | CYS77 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE FAD C 401 |
Chain | Residue |
B | SER38 |
C | ARG93 |
C | LEU94 |
C | TYR95 |
C | SER96 |
C | CYS114 |
C | VAL115 |
C | LYS116 |
C | LEU118 |
C | TYR120 |
C | GLY130 |
C | VAL131 |
C | CYS132 |
C | SER133 |
C | THR172 |
C | TYR314 |
C | HOH509 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES D 101 |
Chain | Residue |
D | SER38 |
D | CYS39 |
D | ARG40 |
D | GLY42 |
D | SER43 |
D | CYS44 |
D | CYS47 |
D | LEU75 |
D | CYS77 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE FAD E 401 |
Chain | Residue |
E | ARG93 |
E | LEU94 |
E | TYR95 |
E | SER96 |
E | CYS114 |
E | VAL115 |
E | LYS116 |
E | LEU118 |
E | TYR120 |
E | GLY130 |
E | VAL131 |
E | CYS132 |
E | SER133 |
E | THR172 |
E | TYR314 |
E | HOH507 |
H | SER38 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES F 101 |
Chain | Residue |
F | SER38 |
F | CYS39 |
F | ARG40 |
F | GLY42 |
F | SER43 |
F | CYS44 |
F | CYS47 |
F | LEU75 |
F | CYS77 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE FAD G 401 |
Chain | Residue |
F | SER38 |
G | ARG93 |
G | LEU94 |
G | TYR95 |
G | SER96 |
G | CYS114 |
G | VAL115 |
G | LYS116 |
G | LEU118 |
G | TYR120 |
G | GLY130 |
G | VAL131 |
G | CYS132 |
G | SER133 |
G | THR172 |
G | GLU312 |
G | TYR314 |
G | HOH503 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FES H 101 |
Chain | Residue |
H | GLY42 |
H | SER43 |
H | CYS44 |
H | CYS47 |
H | LEU75 |
H | CYS77 |
H | SER38 |
H | CYS39 |
H | ARG40 |
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. CRAGSCSSC |
Chain | Residue | Details |
B | CYS39-CYS47 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
B | CYS39 | |
F | CYS44 | |
F | CYS47 | |
F | CYS77 | |
H | CYS39 | |
H | CYS44 | |
H | CYS47 | |
H | CYS77 | |
B | CYS44 | |
B | CYS47 | |
B | CYS77 | |
D | CYS39 | |
D | CYS44 | |
D | CYS47 | |
D | CYS77 | |
F | CYS39 |