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1YZX

Crystal structure of human kappa class glutathione transferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004602molecular_functionglutathione peroxidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0030855biological_processepithelial cell differentiation
A0043231cellular_componentintracellular membrane-bounded organelle
A0070062cellular_componentextracellular exosome
A0098869biological_processcellular oxidant detoxification
B0004364molecular_functionglutathione transferase activity
B0004602molecular_functionglutathione peroxidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0030855biological_processepithelial cell differentiation
B0043231cellular_componentintracellular membrane-bounded organelle
B0070062cellular_componentextracellular exosome
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GSF A 301
ChainResidue
ASER16
AGLY199
ASER200
AASP201
AHOH401
AHOH402
AHOH495
AHOH522
BLYS62
BARG202
APRO17
ATYR18
AILE44
AMET48
AASN53
AGLY182
ALEU183
APHE198

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GSF B 1301
ChainResidue
ALYS62
AARG202
BSER16
BPRO17
BTYR18
BILE44
BMET48
BASN53
BMET91
BGLY182
BLEU183
BPHE198
BGLY199
BSER200
BASP201
BHOH447
BHOH456
BHOH494
BHOH517
BHOH562

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16081649
ChainResidueDetails
APRO17
ALYS54
APRO184
AASP201
BPRO17
BLYS54
BPRO184
BASP201

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9DCM2
ChainResidueDetails
AASP50
AALA145
BASP50
BALA145

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALEU72
AGLU170
BLEU72
BGLU170

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCM2
ChainResidueDetails
AASP86
AASN166
BASP86
BASN166

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCM2
ChainResidueDetails
AALA117
AILE159
BALA117
BILE159

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PDB entries from 2024-10-30

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