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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 Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P09488
ChainResidueDetails
ATYR8
BGLN73
AARG44
ALYS51
AASN60
AGLN73
BTYR8
BARG44
BLYS51
BASN60

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR117
BTYR117

222036

PDB entries from 2024-07-03

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