1ZKQ
Crystal structure of mouse thioredoxin reductase type 2
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000305 | biological_process | response to oxygen radical |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0006979 | biological_process | response to oxidative stress |
A | 0007507 | biological_process | heart development |
A | 0010035 | biological_process | obsolete response to inorganic substance |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0030097 | biological_process | hemopoiesis |
A | 0030424 | cellular_component | axon |
A | 0030425 | cellular_component | dendrite |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043025 | cellular_component | neuronal cell body |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | GLY46 |
A | LYS94 |
A | LYS158 |
A | ALA159 |
A | ALA187 |
A | THR188 |
A | GLY189 |
A | SER208 |
A | TYR228 |
A | VAL229 |
A | ARG318 |
A | SER49 |
A | THR324 |
A | LEU325 |
A | GLY358 |
A | ASP359 |
A | GLU366 |
A | LEU367 |
A | THR368 |
A | PRO369 |
A | PHE400 |
A | HIS497 |
A | GLY50 |
A | HOH605 |
A | HOH617 |
A | HOH622 |
A | ASP69 |
A | TYR70 |
A | GLY84 |
A | THR85 |
A | CYS86 |
A | CYS91 |
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 | GLY83-PRO93 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | HIS497 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP41 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS79 | |
A | LYS175 | |
A | LYS329 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CROSSLNK: Cysteinyl-selenocysteine (Cys-Sec) => ECO:0000250 |
Chain | Residue | Details |
A | CYS522 | |
A | CYS523 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | CYS86 | |
A | CYS91 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1get |
Chain | Residue | Details |
A | HIS497 | |
A | GLU502 |