7C3F
Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
B | 0015979 | biological_process | photosynthesis |
C | 0015035 | molecular_function | protein-disulfide reductase activity |
D | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
E | 0015979 | biological_process | photosynthesis |
F | 0015035 | molecular_function | protein-disulfide reductase activity |
G | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
H | 0015979 | biological_process | photosynthesis |
I | 0015035 | molecular_function | protein-disulfide reductase activity |
J | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
K | 0015979 | biological_process | photosynthesis |
L | 0015035 | molecular_function | protein-disulfide reductase activity |
M | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
N | 0015979 | biological_process | photosynthesis |
O | 0015035 | molecular_function | protein-disulfide reductase activity |
P | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
Q | 0015979 | biological_process | photosynthesis |
R | 0015035 | molecular_function | protein-disulfide reductase activity |
S | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
T | 0015979 | biological_process | photosynthesis |
U | 0015035 | molecular_function | protein-disulfide reductase activity |
V | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
W | 0015035 | molecular_function | protein-disulfide reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue SF4 A 201 |
Chain | Residue |
A | CYS54 |
A | CYS73 |
A | CYS75 |
A | MET78 |
A | CYS84 |
A | HIS85 |
A | CYS86 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue NA A 202 |
Chain | Residue |
A | THR35 |
A | MET87 |
A | LEU88 |
A | PHE28 |
A | CYS29 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue NA C 201 |
Chain | Residue |
C | SER16 |
C | THR17 |
C | SER20 |
D | MET115 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue SF4 D 201 |
Chain | Residue |
D | CYS54 |
D | CYS73 |
D | CYS75 |
D | MET78 |
D | CYS84 |
D | HIS85 |
D | CYS86 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue NA D 202 |
Chain | Residue |
D | PHE28 |
D | CYS29 |
D | THR35 |
D | MET87 |
D | LEU88 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA E 201 |
Chain | Residue |
E | VAL46 |
E | TYR47 |
E | HIS48 |
E | VAL49 |
E | VAL52 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue SF4 G 201 |
Chain | Residue |
G | CYS54 |
G | CYS73 |
G | CYS75 |
G | MET78 |
G | CYS84 |
G | HIS85 |
G | CYS86 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue NA G 202 |
Chain | Residue |
G | PHE28 |
G | CYS29 |
G | THR35 |
G | MET87 |
G | LEU88 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue SF4 J 201 |
Chain | Residue |
J | CYS54 |
J | CYS73 |
J | CYS75 |
J | MET78 |
J | CYS84 |
J | HIS85 |
J | CYS86 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue NA J 202 |
Chain | Residue |
J | PHE28 |
J | CYS29 |
J | THR35 |
J | MET87 |
J | LEU88 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue NA L 201 |
Chain | Residue |
L | ASP15 |
L | SER16 |
L | TRP18 |
L | ASP19 |
O | HOH310 |
O | HOH347 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue SF4 M 201 |
Chain | Residue |
M | CYS54 |
M | CYS73 |
M | CYS75 |
M | MET78 |
M | CYS84 |
M | HIS85 |
M | CYS86 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue NA M 202 |
Chain | Residue |
M | PHE28 |
M | CYS29 |
M | THR35 |
M | MET87 |
M | LEU88 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue NA O 201 |
Chain | Residue |
M | HIS58 |
O | THR66 |
O | ASP67 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue SF4 P 201 |
Chain | Residue |
P | CYS54 |
P | CYS73 |
P | CYS75 |
P | MET78 |
P | CYS84 |
P | HIS85 |
P | CYS86 |
P | HOH312 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue NA P 202 |
Chain | Residue |
P | ARG57 |
P | HIS58 |
Q | SER77 |
R | ARG79 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue SF4 S 201 |
Chain | Residue |
S | CYS54 |
S | CYS73 |
S | CYS75 |
S | MET78 |
S | CYS84 |
S | HIS85 |
S | CYS86 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
C | CYS38 | |
O | SER41 | |
R | CYS38 | |
R | SER41 | |
U | CYS38 | |
U | SER41 | |
W | CYS38 | |
W | SER41 | |
C | SER41 | |
F | CYS38 | |
F | SER41 | |
I | CYS38 | |
I | SER41 | |
L | CYS38 | |
L | SER41 | |
O | CYS38 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | SITE: Deprotonates C-terminal active site Cys => ECO:0000250 |
Chain | Residue | Details |
C | ASP32 | |
G | CYS73 | |
G | CYS75 | |
G | CYS84 | |
J | CYS54 | |
J | CYS73 | |
J | CYS75 | |
J | CYS84 | |
M | CYS54 | |
M | CYS73 | |
M | CYS75 | |
F | ASP32 | |
M | CYS84 | |
P | CYS54 | |
P | CYS73 | |
P | CYS75 | |
P | CYS84 | |
S | CYS54 | |
S | CYS73 | |
S | CYS75 | |
S | CYS84 | |
V | CYS54 | |
I | ASP32 | |
V | CYS73 | |
V | CYS75 | |
V | CYS84 | |
L | ASP32 | |
O | ASP32 | |
R | ASP32 | |
U | ASP32 | |
W | ASP32 | |
G | CYS54 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | SITE: Contributes to redox potential value => ECO:0000250 |
Chain | Residue | Details |
C | GLY39 | |
O | PRO40 | |
R | GLY39 | |
R | PRO40 | |
U | GLY39 | |
U | PRO40 | |
W | GLY39 | |
W | PRO40 | |
C | PRO40 | |
F | GLY39 | |
F | PRO40 | |
I | GLY39 | |
I | PRO40 | |
L | GLY39 | |
L | PRO40 | |
O | GLY39 |