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3DH9

Crystal Structure of Drosophila Thioredoxin Reductase, wild-type

Functional Information from GO Data
ChainGOidnamespacecontents
A0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
B0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0045454biological_processcell redox homeostasis
B0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
AILE15
ACYS57
AGLY61
ACYS62
ALYS65
AGLY128
ALEU129
AGLY130
AALA157
AGLY159
ATYR197
AGLY16
AARG287
ALEU290
AGLY325
AASP326
AGLU333
ALEU334
ATHR335
APRO336
BHIS464
AGLY18
ASER19
AALA20
AASP39
APHE40
AGLY55
ATHR56

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD B 500
ChainResidue
AHIS464
BGLY16
BGLY18
BSER19
BALA20
BASP39
BPHE40
BGLY55
BTHR56
BCYS57
BGLY61
BCYS62
BLYS65
BGLY128
BLEU129
BGLY130
BTYR197
BARG287
BLEU290
BGLY325
BASP326
BGLU333
BLEU334
BTHR335
BPRO336

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP
ChainResidueDetails
AGLY54-PRO64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17385893","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17385893","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS62
ACYS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BCYS62
BCYS57

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AGLU469
AHIS464

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
BGLU469
BHIS464

247536

PDB entries from 2026-01-14

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