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2H8A

Structure of Microsomal Glutathione Transferase 1 in Complex with Glutathione

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
A0010243biological_processresponse to organonitrogen compound
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 218
ChainResidue
AARG73
AGLU80
ALEU124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:16806268
ChainResidueDetails
ALEU3-ASN9
APRO97-LEU99

site_idSWS_FT_FI2
Number of Residues98
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLU10-THR33
AARG63-GLY96
ASER100-PRO123
AARG129-LEU148

site_idSWS_FT_FI3
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16806268
ChainResidueDetails
AALA34-LEU62
ALEU124-ASN128

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16806268
ChainResidueDetails
ALEU38
AARG73
AALA74
ALEU76
AASN81
ALEU121

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Activates the enzyme when modified in vitro => ECO:0000269|PubMed:11106493
ChainResidueDetails
AALA50

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q91VS7
ChainResidueDetails
AVAL42
AGLY55
ALYS60

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine; in vitro => ECO:0000269|PubMed:16314419
ChainResidueDetails
ASER93

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PDB entries from 2024-05-01

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