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1LBK

Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
B0004364molecular_functionglutathione transferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
AASN66
BHOH506
BHOH507
BHOH553
BHOH633
AARG70
AASP94
AGLU97
AHOH530
BASN66
BARG70
BASP94
BGLU97

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 501
ChainResidue
ATRP28
AGLU30
APHE192
AGLU197
AHOH673
BHOH537

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES B 502
ChainResidue
AASP171
BTRP28
BGLU30
BPHE192
BGLU197
BHOH510

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GSH B 503
ChainResidue
AASP98
BTYR7
BPHE8
BARG13
BTRP38
BLYS44
BGLY50
BGLN51
BLEU52
BPRO53
BGLN64
BSER65
BGLU205
BHOH513
BHOH520
BHOH551
BHOH619
BHOH643
BHOH682
BHOH727

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GSH A 504
ChainResidue
ATYR7
APHE8
AARG13
ATRP38
ALYS44
AGLN51
ALEU52
APRO53
AGLN64
ASER65
AGLU205
AHOH516
AHOH523
AHOH525
AHOH538
AHOH604
AHOH620
AHOH665
BASP98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1522586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19396894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19808963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9012673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9245401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9351803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9398518","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16421451","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19618965","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues158
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues242
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by EGFR","evidences":[{"source":"PubMed","id":"19254954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P19157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR7

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR7

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PDB entries from 2025-12-24

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