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5UEH

Structure of GSTO1 covalently conjugated to quinolinic acid fluorosulfate

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 Residues10
Detailsbinding site for residue 85P A 301
ChainResidue
AMET29
AHOH563
APHE31
ALEU56
AVAL127
AILE131
AARG183
AALA186
APHE225
ATYR229

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG39
AHIS49
AVAL51
ALEU215
AHOH421
AHOH510
AHOH515
AHOH532

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG30
ALYS136
AHOH421
AHOH459
AHOH473
AHOH490
AHOH498
AHOH515

site_idAC4
Number of Residues7
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLU21
AGLY22
ASER78
AGLN79
AHOH407
AHOH409
AHOH435

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 305
ChainResidue
AARG48
ALYS200

site_idAC6
Number of Residues2
Detailsbinding site for residue SO4 A 306
ChainResidue
ASER129
AARG132

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL A 307
ChainResidue
ATYR84
ACYS112
AHOH402
AHOH416
AHOH518

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

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PDB entries from 2024-07-17

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