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3M9J

Crystal structure of human thioredoxin C69/73S double mutant, reduced form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0003723molecular_functionRNA binding
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009314biological_processresponse to radiation
A0015035molecular_functionprotein-disulfide reductase activity
A0032148biological_processactivation of protein kinase B activity
A0033138biological_processpositive regulation of peptidyl-serine phosphorylation
A0042803molecular_functionprotein homodimerization activity
A0043388biological_processpositive regulation of DNA binding
A0045454biological_processcell redox homeostasis
A0046826biological_processnegative regulation of protein export from nucleus
A0047134molecular_functionprotein-disulfide reductase (NAD(P)H) activity
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0055114biological_processobsolete oxidation-reduction process
A0061692biological_processcellular detoxification of hydrogen peroxide
A0070062cellular_componentextracellular exosome
A0071731biological_processresponse to nitric oxide
A2000170biological_processpositive regulation of peptidyl-cysteine S-nitrosylation
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0003723molecular_functionRNA binding
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009314biological_processresponse to radiation
B0015035molecular_functionprotein-disulfide reductase activity
B0032148biological_processactivation of protein kinase B activity
B0033138biological_processpositive regulation of peptidyl-serine phosphorylation
B0042803molecular_functionprotein homodimerization activity
B0043388biological_processpositive regulation of DNA binding
B0045454biological_processcell redox homeostasis
B0046826biological_processnegative regulation of protein export from nucleus
B0047134molecular_functionprotein-disulfide reductase (NAD(P)H) activity
B0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0055114biological_processobsolete oxidation-reduction process
B0061692biological_processcellular detoxification of hydrogen peroxide
B0070062cellular_componentextracellular exosome
B0071731biological_processresponse to nitric oxide
B2000170biological_processpositive regulation of peptidyl-cysteine S-nitrosylation
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 Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9108029
ChainResidueDetails
ACYS32
ACYS35
BCYS32
BCYS35

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Deprotonates C-terminal active site Cys => ECO:0000305
ChainResidueDetails
AASP26
BASP26

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Contributes to redox potential value => ECO:0000305
ChainResidueDetails
AGLY33
APRO34
BGLY33
BPRO34

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS3
ALYS39
BLYS3
BLYS39

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P10639
ChainResidueDetails
ALYS8
BLYS8

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17260951
ChainResidueDetails
ACYS62
ASER69
BCYS62
BSER69

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900
ChainResidueDetails
ASER73
BSER73

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P10639
ChainResidueDetails
ALYS94
BLYS94

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PDB entries from 2024-06-12

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