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3KD0

Human thioredoxin C35S,C62S,C69S,C73S mutant showing cadmium chloride bound to the active site

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 PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 106
ChainResidue
AMET74
AASN93
ACD108

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 107
ChainResidue
AMET74
ALYS96
ACD108

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 108
ChainResidue
ACL107
ACL109
ACYS32
AMET74
ACL106

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 109
ChainResidue
AASN93
ALYS96
ACD108
AHOH152

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 110
ChainResidue
AGLU95
AGLU95
AHOH139
AHOH139

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9108029
ChainResidueDetails
ACYS32
ASER35

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Deprotonates C-terminal active site Cys => ECO:0000305
ChainResidueDetails
AASP26

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to redox potential value => ECO:0000305
ChainResidueDetails
AGLY33
APRO34

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS3
ALYS39

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P10639
ChainResidueDetails
ALYS8

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17260951
ChainResidueDetails
ASER62
ASER69

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900
ChainResidueDetails
ASER73

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P10639
ChainResidueDetails
ALYS94

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PDB entries from 2024-10-09

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