Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TKS

Crystal structure of full-length human peroxiredoxin 4 in three different redox states

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0007252biological_processI-kappaB phosphorylation
A0007283biological_processspermatogenesis
A0008379molecular_functionthioredoxin peroxidase activity
A0008584biological_processmale gonad development
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0022417biological_processprotein maturation by protein folding
A0030198biological_processextracellular matrix organization
A0034774cellular_componentsecretory granule lumen
A0042744biological_processhydrogen peroxide catabolic process
A0042802molecular_functionidentical protein binding
A0045454biological_processcell redox homeostasis
A0051920molecular_functionperoxiredoxin activity
A0060090molecular_functionmolecular adaptor activity
A0070062cellular_componentextracellular exosome
A0072593biological_processreactive oxygen species metabolic process
A0098869biological_processcellular oxidant detoxification
A0140313molecular_functionmolecular sequestering activity
A0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
A1904813cellular_componentficolin-1-rich granule lumen
A2000255biological_processnegative regulation of male germ cell proliferation
B0004601molecular_functionperoxidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0007252biological_processI-kappaB phosphorylation
B0007283biological_processspermatogenesis
B0008379molecular_functionthioredoxin peroxidase activity
B0008584biological_processmale gonad development
B0016209molecular_functionantioxidant activity
B0016491molecular_functionoxidoreductase activity
B0022417biological_processprotein maturation by protein folding
B0030198biological_processextracellular matrix organization
B0034774cellular_componentsecretory granule lumen
B0042744biological_processhydrogen peroxide catabolic process
B0042802molecular_functionidentical protein binding
B0045454biological_processcell redox homeostasis
B0051920molecular_functionperoxiredoxin activity
B0060090molecular_functionmolecular adaptor activity
B0070062cellular_componentextracellular exosome
B0072593biological_processreactive oxygen species metabolic process
B0098869biological_processcellular oxidant detoxification
B0140313molecular_functionmolecular sequestering activity
B0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
B1904813cellular_componentficolin-1-rich granule lumen
B2000255biological_processnegative regulation of male germ cell proliferation
C0004601molecular_functionperoxidase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005829cellular_componentcytosol
C0006979biological_processresponse to oxidative stress
C0007252biological_processI-kappaB phosphorylation
C0007283biological_processspermatogenesis
C0008379molecular_functionthioredoxin peroxidase activity
C0008584biological_processmale gonad development
C0016209molecular_functionantioxidant activity
C0016491molecular_functionoxidoreductase activity
C0022417biological_processprotein maturation by protein folding
C0030198biological_processextracellular matrix organization
C0034774cellular_componentsecretory granule lumen
C0042744biological_processhydrogen peroxide catabolic process
C0042802molecular_functionidentical protein binding
C0045454biological_processcell redox homeostasis
C0051920molecular_functionperoxiredoxin activity
C0060090molecular_functionmolecular adaptor activity
C0070062cellular_componentextracellular exosome
C0072593biological_processreactive oxygen species metabolic process
C0098869biological_processcellular oxidant detoxification
C0140313molecular_functionmolecular sequestering activity
C0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
C1904813cellular_componentficolin-1-rich granule lumen
C2000255biological_processnegative regulation of male germ cell proliferation
D0004601molecular_functionperoxidase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005829cellular_componentcytosol
D0006979biological_processresponse to oxidative stress
D0007252biological_processI-kappaB phosphorylation
D0007283biological_processspermatogenesis
D0008379molecular_functionthioredoxin peroxidase activity
D0008584biological_processmale gonad development
D0016209molecular_functionantioxidant activity
D0016491molecular_functionoxidoreductase activity
D0022417biological_processprotein maturation by protein folding
D0030198biological_processextracellular matrix organization
D0034774cellular_componentsecretory granule lumen
D0042744biological_processhydrogen peroxide catabolic process
D0042802molecular_functionidentical protein binding
D0045454biological_processcell redox homeostasis
D0051920molecular_functionperoxiredoxin activity
D0060090molecular_functionmolecular adaptor activity
D0070062cellular_componentextracellular exosome
D0072593biological_processreactive oxygen species metabolic process
D0098869biological_processcellular oxidant detoxification
D0140313molecular_functionmolecular sequestering activity
D0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
D1904813cellular_componentficolin-1-rich granule lumen
D2000255biological_processnegative regulation of male germ cell proliferation
E0004601molecular_functionperoxidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005783cellular_componentendoplasmic reticulum
E0005829cellular_componentcytosol
E0006979biological_processresponse to oxidative stress
E0007252biological_processI-kappaB phosphorylation
E0007283biological_processspermatogenesis
E0008379molecular_functionthioredoxin peroxidase activity
E0008584biological_processmale gonad development
E0016209molecular_functionantioxidant activity
E0016491molecular_functionoxidoreductase activity
E0022417biological_processprotein maturation by protein folding
E0030198biological_processextracellular matrix organization
E0034774cellular_componentsecretory granule lumen
E0042744biological_processhydrogen peroxide catabolic process
E0042802molecular_functionidentical protein binding
E0045454biological_processcell redox homeostasis
E0051920molecular_functionperoxiredoxin activity
E0060090molecular_functionmolecular adaptor activity
E0070062cellular_componentextracellular exosome
E0072593biological_processreactive oxygen species metabolic process
E0098869biological_processcellular oxidant detoxification
E0140313molecular_functionmolecular sequestering activity
E0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
E1904813cellular_componentficolin-1-rich granule lumen
E2000255biological_processnegative regulation of male germ cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PER A 235
ChainResidue
AARG163
ALEU182
AHOH281
AHOH282
AHOH304

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PER C 235
ChainResidue
CHOH374
CPHE85
CVAL86
CCSD87
CARG163

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PER D 235
ChainResidue
DPHE85
DVAL86
DCSD87
DARG163
DHOH241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000305|PubMed:12059788, ECO:0000305|PubMed:21916849
ChainResidueDetails
ECYS87
DCSD87

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon