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1F3A

CRYSTAL STRUCTURE OF MGSTA1-1 IN COMPLEX WITH GSH

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004601molecular_functionperoxidase activity
A0004769molecular_functionsteroid delta-isomerase activity
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006693biological_processprostaglandin metabolic process
A0006749biological_processglutathione metabolic process
A0006805biological_processxenobiotic metabolic process
A0009617biological_processresponse to bacterium
A0016740molecular_functiontransferase activity
A0016853molecular_functionisomerase activity
A0035634biological_processresponse to stilbenoid
A0035731molecular_functiondinitrosyl-iron complex binding
A0042803molecular_functionprotein homodimerization activity
A0043295molecular_functionglutathione binding
A0098869biological_processcellular oxidant detoxification
A1901687biological_processglutathione derivative biosynthetic process
B0004364molecular_functionglutathione transferase activity
B0004601molecular_functionperoxidase activity
B0004769molecular_functionsteroid delta-isomerase activity
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006693biological_processprostaglandin metabolic process
B0006749biological_processglutathione metabolic process
B0006805biological_processxenobiotic metabolic process
B0009617biological_processresponse to bacterium
B0016740molecular_functiontransferase activity
B0016853molecular_functionisomerase activity
B0035634biological_processresponse to stilbenoid
B0035731molecular_functiondinitrosyl-iron complex binding
B0042803molecular_functionprotein homodimerization activity
B0043295molecular_functionglutathione binding
B0098869biological_processcellular oxidant detoxification
B1901687biological_processglutathione derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSH A 224
ChainResidue
ATYR8
AHOH498
AHOH503
AHOH611
AHOH686
AHOH754
BASP100
BARG130
BHOH422
AARG14
ALYS44
AGLN53
AVAL54
APRO55
AGLN66
ATHR67
AHOH382

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GSH B 226
ChainResidue
AASP100
AARG130
BARG14
BLYS44
BASP52
BGLN53
BVAL54
BPRO55
BGLN66
BTHR67
BHOH345
BHOH464
BHOH598
BHOH636

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:11027134
ChainResidueDetails
APHE9
BPHE9

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11027134
ChainResidueDetails
ALYS45
AVAL54
ATHR67
BLYS45
BVAL54
BTHR67

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P80894
ChainResidueDetails
AALA1
BALA1

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed => ECO:0000250|UniProtKB:P30115
ChainResidueDetails
AGLY2
BGLY2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P30115
ChainResidueDetails
APRO4
BPRO4

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR8

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR8

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PDB entries from 2024-07-24

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