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2X8C

Thioredoxin glutathione reductase from Schistosoma mansoni with the reduced C-terminal end

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0046872molecular_functionmetal ion binding
A0050660molecular_functionflavin adenine dinucleotide binding
A0098869biological_processcellular oxidant detoxification
B0000166molecular_functionnucleotide binding
B0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0034599biological_processcellular response to oxidative stress
B0045454biological_processcell redox homeostasis
B0046872molecular_functionmetal ion binding
B0050660molecular_functionflavin adenine dinucleotide binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD A 1599
ChainResidue
AGLY114
ATHR153
ACYS154
AVAL157
AGLY158
ACYS159
ALYS162
AALA226
AGLY228
AALA256
ATHR257
AGLY115
AGLY258
ATYR296
AARG393
AVAL400
AGLY432
AASP433
AGLN440
ALEU441
ATHR442
APRO443
AGLY116
BHIS571
ASER117
AGLY118
ALEU136
AASP137
ATYR138
AGLY152

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 1595
ChainResidue
ALEU320
AGLN326
AGLY333
AASP334
ALYS345

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGE A 1596
ChainResidue
ASER172
AHIS173
AGLU176
AALA306
ASER307
ATYR335
AHIS339

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PEG A 1597
ChainResidue
AASP488
AGLU491
ALYS492

site_idAC5
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD B 1599
ChainResidue
AHIS571
BILE113
BGLY114
BGLY115
BGLY116
BSER117
BGLY118
BLEU136
BASP137
BTYR138
BVAL139
BGLY152
BTHR153
BCYS154
BVAL157
BGLY158
BCYS159
BLYS162
BALA226
BGLY228
BALA256
BTHR257
BGLY258
BTYR296
BARG393
BVAL400
BGLY432
BASP433
BGLN440
BLEU441
BTHR442
BPRO443

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGE B 1600
ChainResidue
BLEU320
BGLN326
BASP334
BGLU337

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP
ChainResidueDetails
AGLY151-PRO161

site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. VIlFSktTCPYCKkVkdvL
ChainResidueDetails
AVAL20-LEU38

site_idPS00195
Number of Residues17
DetailsGLUTAREDOXIN_1 Glutaredoxin active site. LFskttCPYCkkVkdvL
ChainResidueDetails
ALEU22-LEU38

226707

PDB entries from 2024-10-30

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