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3R3E

The glutathione bound structure of YqjG, a glutathione transferase homolog from Escherichia coli K-12

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016672molecular_functionoxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
A0042803molecular_functionprotein homodimerization activity
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016672molecular_functionoxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GSH A 400
ChainResidue
ACYS63
ASO4330
AHOH464
ATRP65
ATRP96
AARG130
ATHR132
AVAL133
APRO134
AGLU148
ASER149

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 329
ChainResidue
AARG73
ALYS74
AHOH471

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 330
ChainResidue
ATRP65
AARG68
AGLU148
AALA150
ATYR187
AARG241
AGSH400
AHOH406

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 331
ChainResidue
ATHR35
AALA36
ATHR158
AALA159
AHOH347
AHOH383
AHOH442

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 332
ChainResidue
ALYS261
AHIS262
AHOH342
AHOH468

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 333
ChainResidue
AHIS262
AASP266
ATYR267

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 334
ChainResidue
AGLY168
AASP169
AGLN234
BPRO80

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GSH B 400
ChainResidue
BCYS63
BTRP65
BTRP96
BARG130
BVAL131
BTHR132
BVAL133
BPRO134
BASN147
BGLU148
BSER149
BHOH415

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 329
ChainResidue
BLYS261
BHIS262
BHOH378

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 330
ChainResidue
BTRP65
BARG68
BALA150
BTYR187
BARG241
BHOH415
BHOH423

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 331
ChainResidue
BARG73
BHOH434

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:22955277
ChainResidueDetails
ACYS63
BCYS63

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:22955277
ChainResidueDetails
ATYR195
BTYR195

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22955277, ECO:0000269|Ref.5
ChainResidueDetails
ATRP96
AARG130
AGLU148
BTRP96
BARG130
BGLU148

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Lowers pKa of active site Cys => ECO:0000305
ChainResidueDetails
ATYR253
ATYR296
BTYR253
BTYR296

225158

PDB entries from 2024-09-18

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