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4Q5Q

Crystal Structure of the Glutathione S-transferase Der p 8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0006749biological_processglutathione metabolic process
A0016740molecular_functiontransferase activity
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0006749biological_processglutathione metabolic process
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GSH A 301
ChainResidue
ACYS135

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GSH A 302
ChainResidue
ACYS121
AASP122
ALYS213
AHOH493

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GSH B 301
ChainResidue
BGSH304

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GSH B 302
ChainResidue
BCYS135
BHOH495

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GSH B 303
ChainResidue
BCYS166

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GSH B 304
ChainResidue
AASP107
BTYR8
BTRP9
BTYR14
BTRP47
BLYS51
BASN60
BLEU61
BPRO62
BGLN73
BTHR74
BGSH301
BHOH402
BHOH470
BHOH490
BHOH525

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues174
DetailsDomain: {"description":"GST N-terminal"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues116
DetailsDomain: {"description":"GST C-terminal"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P09488","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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