Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
B | 0045454 | biological_process | cell redox homeostasis |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD A 500 |
Chain | Residue |
A | GLY16 |
A | VAL60 |
A | GLY61 |
A | CYS62 |
A | LYS65 |
A | GLY128 |
A | LEU129 |
A | GLY130 |
A | ALA157 |
A | VAL158 |
A | GLY159 |
A | GLY18 |
A | TYR197 |
A | ARG287 |
A | LEU290 |
A | LEU294 |
A | GLY325 |
A | ASP326 |
A | GLU333 |
A | LEU334 |
A | THR335 |
A | PRO336 |
A | SER19 |
A | HOH601 |
A | HOH621 |
A | HOH626 |
A | HOH628 |
A | HOH669 |
A | HOH769 |
B | HIS464 |
A | ALA20 |
A | ASP39 |
A | PHE40 |
A | GLY55 |
A | THR56 |
A | CYS57 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | HIS464 |
A | ARG473 |
A | HOH698 |
A | HOH773 |
A | HOH825 |
A | HOH924 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | GLY169 |
A | ALA170 |
A | VAL171 |
A | GLU172 |
site_id | AC4 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD B 500 |
Chain | Residue |
A | HIS464 |
B | GLY16 |
B | GLY17 |
B | GLY18 |
B | SER19 |
B | ALA20 |
B | ASP39 |
B | PHE40 |
B | GLY55 |
B | THR56 |
B | CYS57 |
B | VAL60 |
B | GLY61 |
B | CYS62 |
B | LYS65 |
B | GLY128 |
B | LEU129 |
B | GLY130 |
B | VAL158 |
B | GLY159 |
B | TYR197 |
B | ARG287 |
B | LEU290 |
B | GLY325 |
B | ASP326 |
B | GLU333 |
B | LEU334 |
B | THR335 |
B | PRO336 |
B | HOH667 |
B | HOH670 |
B | HOH727 |
B | HOH815 |
B | HOH905 |
B | HOH1003 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | HIS464 |
B | ARG473 |
B | HOH637 |
B | HOH707 |
B | HOH735 |
B | HOH858 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | GLY169 |
B | ALA170 |
B | VAL171 |
B | GLU172 |
Functional Information from PROSITE/UniProt
site_id | PS00076 |
Number of Residues | 11 |
Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP |
Chain | Residue | Details |
A | GLY54-PRO64 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS464 | |
B | HIS464 | |
Chain | Residue | Details |
A | ILE15 | |
A | PRO250 | |
A | ARG287 | |
A | VAL324 | |
A | GLU333 | |
A | PHE367 | |
A | PRO465 | |
B | ILE15 | |
B | LEU38 | |
B | GLY54 | |
B | GLY128 | |
A | LEU38 | |
B | ALA157 | |
B | SER177 | |
B | PHE181 | |
B | TYR197 | |
B | VAL217 | |
B | PRO250 | |
B | ARG287 | |
B | VAL324 | |
B | GLU333 | |
B | PHE367 | |
A | GLY54 | |
B | PRO465 | |
A | GLY128 | |
A | ALA157 | |
A | SER177 | |
A | PHE181 | |
A | TYR197 | |
A | VAL217 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | CYS62 | |
A | CYS57 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
B | CYS62 | |
B | CYS57 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | GLU469 | |
A | HIS464 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
B | GLU469 | |
B | HIS464 | |