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2Q7V

Crystal Structure of Deinococcus Radiodurans Thioredoxin Reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0019430biological_processremoval of superoxide radicals
A0045454biological_processcell redox homeostasis
B0000166molecular_functionnucleotide binding
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0019430biological_processremoval of superoxide radicals
B0045454biological_processcell redox homeostasis
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 348
ChainResidue
AGLY15
AILE46
AASN54
AASP85
AGLU86
AALA118
ATHR119
AGLY120
ACYS145
AGLY283
AASP284
AGLY17
AARG291
AGLN292
ALEU293
ASER296
APRO18
AALA19
ALEU37
AGLU38
ALYS39
AGLY44
AGLN45

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD B 448
ChainResidue
ATYR26
BGLY15
BGLY17
BPRO18
BALA19
BLEU37
BGLU38
BLYS39
BGLY44
BGLN45
BILE46
BSER49
BASN54
BASP85
BGLU86
BALA118
BTHR119
BGLY120
BCYS145
BGLY283
BASP284
BARG291
BGLN292
BLEU293
BSER296

Functional Information from PROSITE/UniProt
site_idPS00573
Number of Residues21
DetailsPYRIDINE_REDOX_2 Pyridine nucleotide-disulphide oxidoreductases class-II active site. CatCDGff..YkgkkVvVIGGGD
ChainResidueDetails
ACYS142-ASP162

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
ACYS142
ACYS145
AASP146

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1tde
ChainResidueDetails
BCYS142
BCYS145
BASP146

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PDB entries from 2025-06-18

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