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5LKD

Crystal structure of the Xi glutathione transferase ECM4 from Saccharomyces cerevisiae in complex with glutathione

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0006749biological_processglutathione metabolic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
A0071555biological_processcell wall organization
A0098869biological_processcellular oxidant detoxification
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0006749biological_processglutathione metabolic process
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
B0071555biological_processcell wall organization
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue GSH A 401
ChainResidue
AARG15
AGLU173
ASER174
AHOH510
AHOH546
ACYS46
ATRP48
ATRP79
AARG155
ATHR157
AVAL158
APRO159
AASN172

site_idAC2
Number of Residues14
Detailsbinding site for residue GSH B 401
ChainResidue
BSER18
BCYS46
BTRP48
BTRP79
BARG155
BTHR157
BVAL158
BPRO159
BASN172
BGLU173
BSER174
BHOH517
BHOH523
BHOH551

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:16709151, ECO:0000269|PubMed:27736955
ChainResidueDetails
ACYS46
BCYS46

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:27736955, ECO:0007744|PDB:5LKD
ChainResidueDetails
AARG15
BVAL158
BGLU173
BSER174
ATRP79
AARG155
AVAL158
AGLU173
ASER174
BARG15
BTRP79
BARG155

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PDB entries from 2024-04-24

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