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6MHD

Glutathione S-Transferase Omega 1 bound to covalent inhibitor 44

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
B0004364molecular_functionglutathione transferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0014810biological_processpositive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0019852biological_processL-ascorbic acid metabolic process
B0042178biological_processxenobiotic catabolic process
B0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
B0050610molecular_functionmethylarsonate reductase activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
B0070062cellular_componentextracellular exosome
B0071243biological_processcellular response to arsenic-containing substance
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue JRD A 401
ChainResidue
AMET29
AACN403
AHOH583
ACYS32
APHE34
ALEU56
AVAL72
AGLY128
AILE131
AARG132
ATYR229

site_idAC2
Number of Residues6
Detailsbinding site for residue MES A 402
ChainResidue
APHE34
AGLU85
ASER86
AHOH509
AHOH530
BGLU118

site_idAC3
Number of Residues5
Detailsbinding site for residue ACN A 403
ChainResidue
APRO33
AVAL127
AGLY128
ATRP180
AJRD401

site_idAC4
Number of Residues6
Detailsbinding site for residue MES B 302
ChainResidue
AGLU118
BPHE34
BLEU71
BVAL72
BGLU85
BSER86

site_idAC5
Number of Residues5
Detailsbinding site for residue ACN B 303
ChainResidue
BPRO33
BPRO124
BVAL127
BTRP180
BJRD301

site_idAC6
Number of Residues14
Detailsbinding site for Di-peptide JRD B 301 and CYS B 32
ChainResidue
BMET29
BARG30
BPHE31
BPRO33
BPHE34
BALA35
BGLU36
BLEU56
BVAL72
BGLY128
BILE131
BTYR229
BACN303
BHOH415

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:10783391
ChainResidueDetails
ACYS32
BCYS32

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:21106529
ChainResidueDetails
ALYS59
AVAL72
AGLU85
BLYS59
BVAL72
BGLU85

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS57
ALYS143
ALYS148
ALYS152
BLYS57
BLYS143
BLYS148
BLYS152

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER129
BSER129

222415

PDB entries from 2024-07-10

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