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3ERG

Crystal structure of Gtt2 from Saccharomyces cerevisiae in complex with glutathione sulfnate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
A0043295molecular_functionglutathione binding
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
B0043295molecular_functionglutathione binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GTS B 234
ChainResidue
BGLY27
BGLU85
BCYS86
BHIS133
BLEU139
BHOH237
BHOH238
BHOH244
BHOH249
BHOH250
BHOH292
BPRO28
BHOH301
BHOH312
BHOH316
BTYR29
BPRO30
BARG32
BHIS58
BLYS59
BTHR71
BVAL72

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GTS A 234
ChainResidue
AGLY27
APRO28
ATYR29
APRO30
AARG32
ALEU53
AHIS58
ATHR71
AVAL72
AGLU85
ACYS86
AGLU121
AHIS133
AHOH235
AHOH252
AHOH262
AHOH279
AHOH318
AHOH323
AHOH330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19851333
ChainResidueDetails
ATYR29
AHIS58
AVAL72
AHIS133
BTYR29
BHIS58
BVAL72
BHIS133

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLU85
BGLU85

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
AASP23

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BASP23

221716

PDB entries from 2024-06-26

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