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1YKC

human glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004602molecular_functionglutathione peroxidase activity
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006749biological_processglutathione metabolic process
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A0016529cellular_componentsarcoplasmic reticulum
A0016740molecular_functiontransferase activity
A0018916biological_processnitrobenzene metabolic process
A0019855molecular_functioncalcium channel inhibitor activity
A0019899molecular_functionenzyme binding
A0042178biological_processxenobiotic catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043295molecular_functionglutathione binding
A0043651biological_processlinoleic acid metabolic process
A0044325molecular_functiontransmembrane transporter binding
A0051122biological_processhepoxilin biosynthetic process
A0055119biological_processrelaxation of cardiac muscle
A0070062cellular_componentextracellular exosome
A0070458biological_processcellular detoxification of nitrogen compound
A0071313biological_processcellular response to caffeine
A0098869biological_processcellular oxidant detoxification
B0004364molecular_functionglutathione transferase activity
B0004602molecular_functionglutathione peroxidase activity
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006749biological_processglutathione metabolic process
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B0016529cellular_componentsarcoplasmic reticulum
B0016740molecular_functiontransferase activity
B0018916biological_processnitrobenzene metabolic process
B0019855molecular_functioncalcium channel inhibitor activity
B0019899molecular_functionenzyme binding
B0042178biological_processxenobiotic catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043295molecular_functionglutathione binding
B0043651biological_processlinoleic acid metabolic process
B0044325molecular_functiontransmembrane transporter binding
B0051122biological_processhepoxilin biosynthetic process
B0055119biological_processrelaxation of cardiac muscle
B0070062cellular_componentextracellular exosome
B0070458biological_processcellular detoxification of nitrogen compound
B0071313biological_processcellular response to caffeine
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GDS A 400
ChainResidue
ATYR6
AGLN71
ASER72
AARG107
AALA111
ATYR115
AARG165
APHE208
AHOH404
AHOH421
AHOH467
ATRP7
AHOH469
AHOH589
BASP105
AGLY11
ALEU12
AARG42
ATRP45
ALYS49
AASN58
ALEU59

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE GDS B 401
ChainResidue
AASP105
AHOH484
BTYR6
BTRP7
BGLY11
BLEU12
BARG42
BTRP45
BLYS49
BASN58
BLEU59
BGLN71
BSER72
BARG107
BALA111
BTYR115
BARG165
BPHE208
BHOH415
BHOH492
BHOH505
BHOH538
BHOH548
BHOH585
BHOH589
BHOH599

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues172
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues236
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16549767","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19808963","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P08010","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08010","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR6

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR6

239803

PDB entries from 2025-08-06

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