Structure of PDB 3dgz Chain A

Receptor sequence
>3dgzA (length=482) Species: 10090 (Mus musculus) [Search protein sequence]
QQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGTC
VNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVQHNWKTMAEAVQNHV
KSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLLSAEHIVI
ATGGRPRYPTQVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGF
LTGIGLDTTVMMRSIPLRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKK
LPTNQLQVTWEDHASGKEDTGTFDTVLWAIGRVPETRTLNLEKAGISTNP
KNQKIIVDAQEATSVPHIYAIGDVAEGRPELTPTAIKAGKLLAQRLFGKS
STLMDYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHVEVYHAYYKPLEF
TVADRDASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIKCGAS
YAQVMQTVGIHPTCSEEVVKLHISKRSGLEPT
3D structure
PDB3dgz Crystal Structure of Mouse Mitochondrial Thioredoxin Reductase, C-terminal 3-residue truncation
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L49 C53 C58 K61 Y195 E199 G462 H464 E469
Catalytic site (residue number reindexed from 1) L46 C50 C55 K58 Y192 E196 G459 H461 E466
Enzyme Commision number 1.8.1.9: thioredoxin-disulfide reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0042803 protein homodimerization activity
GO:0050660 flavin adenine dinucleotide binding
Biological Process
GO:0000305 response to oxygen radical
GO:0006979 response to oxidative stress
GO:0007507 heart development
GO:0030097 hemopoiesis
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005739 mitochondrion

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Molecular Function

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Cellular Component
External links
PDB RCSB:3dgz, PDBe:3dgz, PDBj:3dgz
PDBsum3dgz
PubMed
UniProtQ9JLT4|TRXR2_MOUSE Thioredoxin reductase 2, mitochondrial (Gene Name=Txnrd2)

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