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5I9K

The structure of microsomal glutathione transferase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004602molecular_functionglutathione peroxidase activity
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005778cellular_componentperoxisomal membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006749biological_processglutathione metabolic process
A0009410biological_processresponse to xenobiotic stimulus
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0032496biological_processresponse to lipopolysaccharide
A0033327biological_processLeydig cell differentiation
A0034635biological_processglutathione transport
A0042802molecular_functionidentical protein binding
A0043295molecular_functionglutathione binding
A0045177cellular_componentapical part of cell
A0071449biological_processcellular response to lipid hydroperoxide
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GSH A 201
ChainResidue
AARG38
AHIS76
ALEU77

site_idAC2
Number of Residues4
Detailsbinding site for residue PC1 A 202
ChainResidue
AILE105
AVAL136
AVAL140
AMET144

site_idAC3
Number of Residues3
Detailsbinding site for residue PC1 A 203
ChainResidue
APRO124
ATYR116
AALA120

site_idAC4
Number of Residues6
Detailsbinding site for residue PLM A 204
ChainResidue
ALEU30
AILE115
ATHR118
AILE119
ATYR121
ALEU122

site_idAC5
Number of Residues6
Detailsbinding site for residue PLM A 205
ChainResidue
APRO85
AILE89
ALEU92
ATYR93
ALEU149
ALEU153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:16806268
ChainResidueDetails
AASP3-ASP9
AGLY97-ASP99
ALEU149-LEU155

site_idSWS_FT_FI2
Number of Residues98
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AASN10-ALA33
ALEU63-SER96
ALEU100-THR123
AASN129-LEU148

site_idSWS_FT_FI3
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16806268
ChainResidueDetails
ATHR34-PHE62
APRO124-PRO128

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16806268
ChainResidueDetails
AARG38
AARG73
AARG74
AHIS76
AGLU81
ATYR121

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Activates the enzyme when modified in vitro => ECO:0000269|PubMed:11106493
ChainResidueDetails
ACYS50

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91VS7
ChainResidueDetails
ALYS42
ALYS55
ALYS60

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine; in vitro => ECO:0000269|PubMed:16314419
ChainResidueDetails
ATYR93

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PDB entries from 2024-11-06

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