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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

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
A0016209molecular_functionantioxidant activity
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
B0016209molecular_functionantioxidant activity
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
C0016209molecular_functionantioxidant activity
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
D0016209molecular_functionantioxidant activity
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 Residues668
DetailsDomain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"PubMed","id":"22474296","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Cysteine persulfide","evidences":[{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1)","evidences":[{"source":"PubMed","id":"32004955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21209336","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1); alternate","evidences":[{"source":"PubMed","id":"32004955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1); alternate","evidences":[{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1)","evidences":[{"source":"PubMed","id":"36102610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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