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6RWD

Crystal structure of SjGST in complex with GSH and ellagic acid at 1.53 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
B0004364molecular_functionglutathione transferase activity
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue GSH A 301
ChainResidue
ATYR6
ASER67
AHOH422
AHOH476
AHOH488
BASP100
BREF302
BHOH411
ATRP7
ALEU12
ATRP40
ALYS44
AASN53
ALEU54
APRO55
AGLN66

site_idAC2
Number of Residues3
Detailsbinding site for residue NA A 302
ChainResidue
AASP213
ACL303
AHOH527

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 303
ChainResidue
AARG34
ANA302

site_idAC4
Number of Residues19
Detailsbinding site for residue GSH B 301
ChainResidue
AASP100
BTYR6
BTRP7
BLEU12
BTRP40
BLYS44
BASN53
BLEU54
BPRO55
BGLN66
BSER67
BREF302
BHOH404
BHOH431
BHOH452
BHOH463
BHOH472
BHOH513
BHOH532

site_idAC5
Number of Residues14
Detailsbinding site for residue REF B 302
ChainResidue
AASP100
ATYR103
AARG107
AGSH301
BASP100
BTYR103
BARG107
BGSH301
BHOH402
BHOH411
BHOH412
BHOH422
BHOH424
BHOH472

site_idAC6
Number of Residues2
Detailsbinding site for residue NA B 303
ChainResidue
BCL304
BHOH469

site_idAC7
Number of Residues2
Detailsbinding site for residue CL B 304
ChainResidue
BARG34
BNA303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:7538846, ECO:0000305|PubMed:12596270
ChainResidueDetails
ATYR6
ATRP40
AASN53
AGLN66
BTYR6
BTRP40
BASN53
BGLN66

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ATYR110
BTYR110

219140

PDB entries from 2024-05-01

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