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5IA9

The structure of microsomal glutathione transferase 1 in complex with Meisenheimer complex

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 Residues4
Detailsbinding site for residue GTD A 201
ChainResidue
AARG38
ALEU39
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
AALA120
APRO124
ATYR116

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 Residues65
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"16806268","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16806268","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16806268","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VS7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine; in vitro","evidences":[{"source":"PubMed","id":"16314419","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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