Structure of PDB 2nvk Chain X

Receptor sequence

>2nvkX (length=481) Species: 7227 (Drosophila melanogaster)

YDYDLIVIGGGSAGLACAKEAVLNGARVACLDFVKPTPTLGTKWGVGGTC
VNVGCIPKKLMHQASLLGEAVHEAAAYGWNVDDKIKPDWHKLVQSVQNHI
KSVNWVTRVDLRDKKVEYINGLGSFVDSHTLLAKLKSGERTITAQTFVIA
VGGRPRYPDIPGAVEYGITSDDLFSLDREPGKTLVVGAGYIGLECAGFLK
GLGYEPTVMVRSIVLRGFDQQMAELVAASMEERGIPFLRKTVPLSVEKQD
DGKLLVKYKNVETGEESEDVYDTVLWAIGRKGLVDDLNLPNAGVTVQKDK
IPVDSQEATNVANIYAVGDIIYGKPELTPVAVLAGRLLARRLYGGSTQRM
DYKDVATTVFTPLEYACVGLSEEDAVKQFGADEIEVFHGYYKPTEFFIPQ
KSVRYCYLKAVAERHGDQRVYGLHYIGPVAGEVIQGFAAALKSGLTINTL
INTVGIHPTTAEEFTRLAITKRSGLDPTPAS

3D structure

• PDB: 2nvk Structural and Biochemical Studies Reveal Differences in the Catalytic Mechanisms of Mammalian and Drosophila melanogaster Thioredoxin Reductases.
• Chain: X
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V53 C57 C62 S488
• Catalytic site (residue number reindexed from 1): V46 C50 C55 S481
• Enzyme Commision number: 1.8.1.9: thioredoxin-disulfide reductase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	X	I15 G18 S19 A20 D39 F40 T56 G61 C62 K65 L129 G130 V158 Y197 I198 R287 G325 D326 E333 L334 T335	I8 G11 S12 A13 D32 F33 T49 G54 C55 K58 L122 G123 V151 Y190 I191 R280 G318 D319 E326 L327 T328
BS02	NAP	X	G194 A195 R218 S219 R223 A284 I285 G286	G187 A188 R211 S212 R216 A277 I278 G279

Gene Ontology

Molecular Function

• GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
• GO:0016491 oxidoreductase activity
• GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
• GO:0050660 flavin adenine dinucleotide binding

Biological Process

• GO:0045454 cell redox homeostasis

External links

• PDB: RCSB:2nvk, PDBe:2nvk, PDBj:2nvk
• PDBsum: 2nvk
• PubMed: 17385893
• UniProt: P91938|TRXR1_DROME Thioredoxin reductase 1, mitochondrial (Gene Name=Trxr1)