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2NVK

Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster

Functional Information from GO Data
ChainGOidnamespacecontents
X0004791molecular_functionthioredoxin-disulfide reductase (NADPH) activity
X0016491molecular_functionoxidoreductase activity
X0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
X0045454biological_processcell redox homeostasis
X0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD X 489
ChainResidue
XGLY16
XCYS57
XVAL60
XGLY61
XCYS62
XLYS65
XGLY128
XLEU129
XGLY130
XALA157
XVAL158
XGLY17
XGLY159
XTYR197
XILE198
XARG287
XLEU290
XGLY325
XASP326
XGLU333
XLEU334
XTHR335
XGLY18
XPRO336
XHIS464
XHOH492
XHOH498
XHOH514
XHOH517
XHOH523
XHOH566
XSER19
XALA20
XASP39
XPHE40
XGLY55
XTHR56

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NAP X 490
ChainResidue
XGLY194
XALA195
XGLY196
XARG218
XSER219
XARG223
XALA284
XILE285
XGLY286
XARG287
XHOH535
XHOH570
XHOH610

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP
ChainResidueDetails
XGLY54-PRO64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17385893","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
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
XCYS62
XCYS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
XGLU469
XHIS464

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PDB entries from 2026-01-14

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