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5ZWP

Crystal structure of the delta-class glutathione transferase from Musca domestica

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004364molecular_functionglutathione transferase activity
A0016740molecular_functiontransferase activity
B0003824molecular_functioncatalytic activity
B0004364molecular_functionglutathione transferase activity
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue GSH A 301
ChainResidue
ALEU33
AFMT302
AHOH441
AHOH457
AHOH489
AHOH496
AHOH519
AHOH539
AHOH548
AHOH604
AHIS38
AHIS50
ATHR51
AILE52
APRO53
AGLU64
ASER65
AARG66

site_idAC2
Number of Residues8
Detailsbinding site for residue FMT A 302
ChainResidue
APRO11
ATYR105
ATYR113
AGSH301
AHOH422
AHOH451
AHOH555
AHOH570

site_idAC3
Number of Residues5
Detailsbinding site for residue FMT A 303
ChainResidue
AMET101
AGLY102
AHOH418
BMET101
BGLY102

site_idAC4
Number of Residues6
Detailsbinding site for residue FMT A 304
ChainResidue
ATHR103
ALYS106
ASER107
AHOH419
AHOH445
AHOH464

site_idAC5
Number of Residues4
Detailsbinding site for residue FMT A 305
ChainResidue
ATHR139
APHE140
ALYS142
AHOH402

site_idAC6
Number of Residues6
Detailsbinding site for residue FMT A 306
ChainResidue
ATRP193
ATRP197
AHOH416
AHOH429
AHOH470
AHOH473

site_idAC7
Number of Residues5
Detailsbinding site for residue FMT A 307
ChainResidue
ALYS89
AGLY149
AASP150
ASER151
BLYS119

site_idAC8
Number of Residues17
Detailsbinding site for residue GSH B 301
ChainResidue
BLEU33
BHIS38
BHIS50
BTHR51
BILE52
BPRO53
BGLU64
BSER65
BARG66
BMET101
BHOH469
BHOH470
BHOH480
BHOH493
BHOH518
BHOH548
BHOH605

site_idAC9
Number of Residues5
Detailsbinding site for residue FMT B 302
ChainResidue
BLEU6
BLEU33
BGLN34
BHOH407
BHOH475

site_idAD1
Number of Residues5
Detailsbinding site for residue FMT B 303
ChainResidue
APRO48
BARG96
BPHE140
BHOH514
BHOH535

site_idAD2
Number of Residues6
Detailsbinding site for residue FMT B 304
ChainResidue
ALYS119
BLYS89
BGLY149
BASP150
BSER151
BHOH417

site_idAD3
Number of Residues6
Detailsbinding site for residue FMT B 305
ChainResidue
BTRP193
BTRP197
BHOH420
BHOH432
BHOH435
BHOH496

site_idAD4
Number of Residues4
Detailsbinding site for residue FMT B 306
ChainResidue
BMET1
BTYR76
BHOH404
BHOH447

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER9
AHIS50
AGLU64
BSER9
BHIS50
BGLU64

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PDB entries from 2024-07-10

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