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8YS3

Crystal structure of rat thioredoxin, F54L mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009314biological_processresponse to radiation
A0010269biological_processresponse to selenium ion
A0014823biological_processresponse to activity
A0015035molecular_functionprotein-disulfide reductase activity
A0019725biological_processcellular homeostasis
A0019899molecular_functionenzyme binding
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0042803molecular_functionprotein homodimerization activity
A0043025cellular_componentneuronal cell body
A0043388biological_processpositive regulation of DNA binding
A0045454biological_processcell redox homeostasis
A0047134molecular_functionprotein-disulfide reductase [NAD(P)H] activity
A0048678biological_processresponse to axon injury
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0055114biological_processobsolete oxidation-reduction process
A0061692biological_processcellular detoxification of hydrogen peroxide
A0071236biological_processcellular response to antibiotic
A0071333biological_processcellular response to glucose stimulus
A0071455biological_processcellular response to hyperoxia
A0071466biological_processcellular response to xenobiotic stimulus
A0071548biological_processresponse to dexamethasone
A0071731biological_processresponse to nitric oxide
A0097068biological_processresponse to thyroxine
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009314biological_processresponse to radiation
B0010269biological_processresponse to selenium ion
B0014823biological_processresponse to activity
B0015035molecular_functionprotein-disulfide reductase activity
B0019725biological_processcellular homeostasis
B0019899molecular_functionenzyme binding
B0030424cellular_componentaxon
B0030425cellular_componentdendrite
B0042803molecular_functionprotein homodimerization activity
B0043025cellular_componentneuronal cell body
B0043388biological_processpositive regulation of DNA binding
B0045454biological_processcell redox homeostasis
B0047134molecular_functionprotein-disulfide reductase [NAD(P)H] activity
B0048678biological_processresponse to axon injury
B0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0055114biological_processobsolete oxidation-reduction process
B0061692biological_processcellular detoxification of hydrogen peroxide
B0071236biological_processcellular response to antibiotic
B0071333biological_processcellular response to glucose stimulus
B0071455biological_processcellular response to hyperoxia
B0071466biological_processcellular response to xenobiotic stimulus
B0071548biological_processresponse to dexamethasone
B0071731biological_processresponse to nitric oxide
B0097068biological_processresponse to thyroxine
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. VVdFSatWCGPCKmIkpfF
ChainResidueDetails
AVAL24-PHE42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues206
DetailsDomain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"UniProtKB","id":"P10599","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P10639","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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