4TRX
HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF REDUCED RECOMBINANT HUMAN THIOREDOXIN IN SOLUTION
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
A | 0003723 | molecular_function | RNA binding |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009314 | biological_process | response to radiation |
A | 0015035 | molecular_function | protein-disulfide reductase activity |
A | 0033138 | biological_process | positive regulation of peptidyl-serine phosphorylation |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043388 | biological_process | positive regulation of DNA binding |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0046826 | biological_process | negative regulation of protein export from nucleus |
A | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)H) activity |
A | 0051897 | biological_process | positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction |
A | 0055114 | biological_process | obsolete oxidation-reduction process |
A | 0061692 | biological_process | cellular detoxification of hydrogen peroxide |
A | 0070062 | cellular_component | extracellular exosome |
A | 0071731 | biological_process | response to nitric oxide |
A | 2000170 | biological_process | positive regulation of peptidyl-cysteine S-nitrosylation |
Functional Information from PROSITE/UniProt
site_id | PS00194 |
Number of Residues | 19 |
Details | THIOREDOXIN_1 Thioredoxin family active site. VVdFSatWCGPCKmIkpfF |
Chain | Residue | Details |
A | VAL24-PHE42 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:9108029 |
Chain | Residue | Details |
A | GLY33 | |
A | LYS36 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Deprotonates C-terminal active site Cys => ECO:0000305 |
Chain | Residue | Details |
A | PHE27 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Contributes to redox potential value => ECO:0000305 |
Chain | Residue | Details |
A | PRO34 | |
A | CYS35 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | GLN4 | |
A | PRO40 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P10639 |
Chain | Residue | Details |
A | THR9 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17260951 |
Chain | Residue | Details |
A | GLN63 | |
A | GLU70 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900 |
Chain | Residue | Details |
A | THR74 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P10639 |
Chain | Residue | Details |
A | GLU95 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
A | PRO34 | |
A | CYS35 | |
A | CYS32 | |
A | GLY33 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
A | CYS35 | |
A | CYS32 |