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1GP1

THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0004602molecular_functionglutathione peroxidase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006749biological_processglutathione metabolic process
A0006979biological_processresponse to oxidative stress
A0010269biological_processresponse to selenium ion
A0016491molecular_functionoxidoreductase activity
A0019369biological_processarachidonic acid metabolic process
A0019372biological_processlipoxygenase pathway
A0042542biological_processresponse to hydrogen peroxide
A0042744biological_processhydrogen peroxide catabolic process
A0047066molecular_functionphospholipid-hydroperoxide glutathione peroxidase activity
A0070887biological_processcellular response to chemical stimulus
A0098869biological_processcellular oxidant detoxification
A1902905biological_processpositive regulation of supramolecular fiber organization
B0004601molecular_functionperoxidase activity
B0004602molecular_functionglutathione peroxidase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006749biological_processglutathione metabolic process
B0006979biological_processresponse to oxidative stress
B0010269biological_processresponse to selenium ion
B0016491molecular_functionoxidoreductase activity
B0019369biological_processarachidonic acid metabolic process
B0019372biological_processlipoxygenase pathway
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0047066molecular_functionphospholipid-hydroperoxide glutathione peroxidase activity
B0070887biological_processcellular response to chemical stimulus
B0098869biological_processcellular oxidant detoxification
B1902905biological_processpositive regulation of supramolecular fiber organization
Functional Information from PROSITE/UniProt
site_idPS00460
Number of Residues16
DetailsGLUTATHIONE_PEROXID_1 Glutathione peroxidases active site. GKvLLIeNVaSlUGtT
ChainResidueDetails
AGLY33-THR48

site_idPS00763
Number of Residues8
DetailsGLUTATHIONE_PEROXID_2 Glutathione peroxidases signature 2. LGFPCNQF
ChainResidueDetails
ALEU70-PHE77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:O70325
ChainResidueDetails
ASE745
BSE745

site_idSWS_FT_FI2
Number of Residues12
DetailsSITE: Not glycated => ECO:0000269|PubMed:7873592
ChainResidueDetails
ALYS34
BLYS117
BLYS144
BLYS162
ALYS84
ALYS93
ALYS117
ALYS144
ALYS162
BLYS34
BLYS84
BLYS93

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Subject to oxidation and hydroselenide loss to dehydroalanine => ECO:0000250
ChainResidueDetails
ASE745
BSE745

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04041
ChainResidueDetails
ASER30
ASER193
BSER30
BSER193

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P11352
ChainResidueDetails
ALYS84
ALYS110
ALYS144
BLYS84
BLYS110
BLYS144

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11352
ChainResidueDetails
ALYS117
BLYS117

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07203
ChainResidueDetails
ASER197
BSER197

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:7873592
ChainResidueDetails
ALYS110
BLYS110

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 851
ChainResidueDetails
ASE745covalent catalysis, proton shuttle (general acid/base)
AGLN80electrostatic stabiliser
ATRP158proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 851
ChainResidueDetails
BSE745covalent catalysis, proton shuttle (general acid/base)
BGLN80electrostatic stabiliser
BTRP158proton shuttle (general acid/base)

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PDB entries from 2024-04-24

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