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6JI6

Crystal structure of glutathione S-transferase complexed and modified with glutathione

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue GSH A 301
ChainResidue
ATYR7
ASER68
AASP101
ATRS307
AHOH482
AHOH501
AHOH562
AHOH572
AHOH582
AHOH611
AHOH619
ATRP8
ALEU13
ATRP41
ALYS45
AASN54
ALEU55
APRO56
AGLN67

site_idAC2
Number of Residues12
Detailsbinding site for residue GSH A 302
ChainResidue
AGLY84
ACYS85
ALYS87
AGLU88
AGLU91
AASN144
AHOH407
AHOH444
AHOH539
AHOH544
AHOH571
AHOH600

site_idAC3
Number of Residues10
Detailsbinding site for residue GSH A 303
ChainResidue
AARG42
ACYS138
AHIS139
ALYS175
AGSH304
AHOH471
AHOH494
AHOH497
AHOH534
AHOH607

site_idAC4
Number of Residues19
Detailsbinding site for residue GSH A 304
ChainResidue
ASER124
AGLU128
ALYS140
APRO174
ALYS175
ACYS178
AARG182
AGSH303
AHOH406
AHOH410
AHOH418
AHOH429
AHOH433
AHOH437
AHOH467
AHOH588
AHOH596
AHOH597
AHOH618

site_idAC5
Number of Residues7
Detailsbinding site for residue ACT A 305
ChainResidue
AGLY12
ALEU13
ATYR111
AGLN204
ATRS307
AHOH546
AHOH715

site_idAC6
Number of Residues7
Detailsbinding site for residue ACT A 306
ChainResidue
AHIS31
ALEU32
ATYR33
ALYS40
ALYS44
AHOH411
AHOH473

site_idAC7
Number of Residues7
Detailsbinding site for residue TRS A 307
ChainResidue
ATYR7
ATYR111
AGLN207
AGSH301
AACT305
AHOH405
AHOH616

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270
ChainResidueDetails
ATYR7
ATRP41
AASN54
AGLN67

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ATYR111

218853

PDB entries from 2024-04-24

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