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

4DSQ

Crystal structure of peroxiredoxin Ahp1 from Saccharomyces cerevisiae in oxidized form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008379molecular_functionthioredoxin peroxidase activity
A0010038biological_processresponse to metal ion
A0016491molecular_functionoxidoreductase activity
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0045454biological_processcell redox homeostasis
A0050821biological_processprotein stabilization
A0098869biological_processcellular oxidant detoxification
A0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
B0004601molecular_functionperoxidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008379molecular_functionthioredoxin peroxidase activity
B0010038biological_processresponse to metal ion
B0016491molecular_functionoxidoreductase activity
B0034599biological_processcellular response to oxidative stress
B0042744biological_processhydrogen peroxide catabolic process
B0045454biological_processcell redox homeostasis
B0050821biological_processprotein stabilization
B0098869biological_processcellular oxidant detoxification
B0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
C0004601molecular_functionperoxidase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005777cellular_componentperoxisome
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0008379molecular_functionthioredoxin peroxidase activity
C0010038biological_processresponse to metal ion
C0016491molecular_functionoxidoreductase activity
C0034599biological_processcellular response to oxidative stress
C0042744biological_processhydrogen peroxide catabolic process
C0045454biological_processcell redox homeostasis
C0050821biological_processprotein stabilization
C0098869biological_processcellular oxidant detoxification
C0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
D0004601molecular_functionperoxidase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005777cellular_componentperoxisome
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0008379molecular_functionthioredoxin peroxidase activity
D0010038biological_processresponse to metal ion
D0016491molecular_functionoxidoreductase activity
D0034599biological_processcellular response to oxidative stress
D0042744biological_processhydrogen peroxide catabolic process
D0045454biological_processcell redox homeostasis
D0050821biological_processprotein stabilization
D0098869biological_processcellular oxidant detoxification
D0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000305|PubMed:22474296
ChainResidueDetails
ACYS62
BCYS62
CCYS62
DCYS62

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.4
ChainResidueDetails
ASER2
BSER2
CSER2
DSER2

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER28
ASER116
BSER28
BSER116
CSER28
CSER116
DSER28
DSER116

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER59
BSER59
CSER59
DSER59

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1) => ECO:0000305|PubMed:21209336
ChainResidueDetails
ALYS32
BLYS32
CLYS32
DLYS32

site_idSWS_FT_FI6
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
DLYS48
DLYS113
ALYS48
ALYS113
BLYS48
BLYS113
CLYS48
CLYS113

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon