Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EEM

GLUTATHIONE TRANSFERASE FROM HOMO SAPIENS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
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
A0014810biological_processpositive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0019852biological_processL-ascorbic acid metabolic process
A0042178biological_processxenobiotic catabolic process
A0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
A0050610molecular_functionmethylarsonate reductase activity
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
A0070062cellular_componentextracellular exosome
A0071243biological_processcellular response to arsenic-containing substance
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 901
ChainResidue
AARG39
AHIS49
AVAL51
AHOH1009

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 902
ChainResidue
AHOH1137
AGLU21
AGLY22
ASER78
AGLN79
AHOH1021

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GSH A 999
ChainResidue
ACYS32
APHE34
ALEU56
ALYS59
ALEU71
AVAL72
APRO73
AGLU85
ASER86
AHOH1002
AHOH1030
AHOH1043

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:10783391
ChainResidueDetails
ACYS32

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529
ChainResidueDetails
ALYS59
AVAL72
AGLU85

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330
ChainResidueDetails
ASER2

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS57
ALYS143
ALYS148
ALYS152

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER129

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon