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2PMT

GLUTATHIONE TRANSFERASE FROM PROTEUS MIRABILIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0016740molecular_functiontransferase activity
B0004364molecular_functionglutathione transferase activity
B0005737cellular_componentcytoplasm
B0016740molecular_functiontransferase activity
C0004364molecular_functionglutathione transferase activity
C0005737cellular_componentcytoplasm
C0016740molecular_functiontransferase activity
D0004364molecular_functionglutathione transferase activity
D0005737cellular_componentcytoplasm
D0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH A 204
ChainResidue
ASER9
ALYS107
BASN99
BSER103
BGLU104
ACYS10
ALYS35
AGLY50
AGLN51
AVAL52
AGLU65
AGLY66
AHIS106

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH B 204
ChainResidue
AASN99
ASER103
AGLU104
BSER9
BCYS10
BLYS35
BGLY50
BGLN51
BVAL52
BGLU65
BGLY66
BHIS106
BLYS107

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH C 204
ChainResidue
CSER9
CCYS10
CLYS35
CGLY50
CGLN51
CVAL52
CGLU65
CGLY66
CHIS106
CLYS107
DASN99
DSER103
DGLU104

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH D 204
ChainResidue
CASN99
CSER103
CGLU104
DSER9
DCYS10
DLYS35
DGLY50
DGLN51
DVAL52
DGLU65
DGLY66
DHIS106
DLYS107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:9655824
ChainResidueDetails
ACYS10
BGLU65
BASN99
BSER103
CCYS10
CLYS35
CVAL52
CGLU65
CASN99
CSER103
DCYS10
ALYS35
DLYS35
DVAL52
DGLU65
DASN99
DSER103
AVAL52
AGLU65
AASN99
ASER103
BCYS10
BLYS35
BVAL52

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR5

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR5

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
CTYR5

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
DTYR5

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PDB entries from 2024-07-10

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