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1PL2

Crystal structure of human glutathione transferase (GST) A1-1 T68E mutant in complex with decarboxy-glutathione

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004601molecular_functionperoxidase activity
A0004602molecular_functionglutathione peroxidase activity
A0004769molecular_functionsteroid delta-isomerase activity
A0005504molecular_functionfatty acid binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0006805biological_processxenobiotic metabolic process
A0016740molecular_functiontransferase activity
A0016853molecular_functionisomerase activity
A0030855biological_processepithelial cell differentiation
A0043651biological_processlinoleic acid metabolic process
A0070062cellular_componentextracellular exosome
A0098869biological_processcellular oxidant detoxification
A1901687biological_processglutathione derivative biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0004601molecular_functionperoxidase activity
B0004602molecular_functionglutathione peroxidase activity
B0004769molecular_functionsteroid delta-isomerase activity
B0005504molecular_functionfatty acid binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0006805biological_processxenobiotic metabolic process
B0016740molecular_functiontransferase activity
B0016853molecular_functionisomerase activity
B0030855biological_processepithelial cell differentiation
B0043651biological_processlinoleic acid metabolic process
B0070062cellular_componentextracellular exosome
B0098869biological_processcellular oxidant detoxification
B1901687biological_processglutathione derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 601
ChainResidue
BPRO56
BGLU68
BABY655
BHOH676

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 602
ChainResidue
APRO56
AGLU68
AABY654

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ABY A 654
ChainResidue
AGLN54
AVAL55
AGLN67
ALEU107
AVAL111
AMET208
APHE220
ACL602
AHOH806
AHOH880
BASP101
BARG131
ATYR9
AARG45

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ABY B 655
ChainResidue
AASP101
AARG131
BTYR9
BARG45
BGLN54
BVAL55
BGLN67
BLEU107
BVAL111
BMET208
BPHE220
BCL601
BHOH828

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16421451, ECO:0000269|PubMed:19618965
ChainResidueDetails
ATYR9
AARG45
AGLN54
AGLN67
BTYR9
BARG45
BGLN54
BGLN67

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P80894
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P30115
ChainResidueDetails
ALYS4
BLYS4

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR9

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR9

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PDB entries from 2024-05-01

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