Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ERV

HUMAN THIOREDOXIN MUTANT WITH CYS 73 REPLACED BY SER (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
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
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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9108029
ChainResidueDetails
AGLY33
ALYS36

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Deprotonates C-terminal active site Cys => ECO:0000305
ChainResidueDetails
APHE27

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to redox potential value => ECO:0000305
ChainResidueDetails
APRO34
ACYS35

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AGLN4
APRO40

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P10639
ChainResidueDetails
ATHR9

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17260951
ChainResidueDetails
AGLN63
AGLU70

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900
ChainResidueDetails
AMET74

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P10639
ChainResidueDetails
AGLU95

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
APRO34
ACYS35
ACYS32
AGLY33

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS35
ACYS32

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon