Structure of PDB 1zdl Chain A

Receptor sequence
>1zdlA (length=484) Species: 10090 (Mus musculus) [Search protein sequence]
QSFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGTCV
NVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVQHNWKTMAEAVQNHVK
SLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLLSAEHIVIA
TGGRPRYPTQVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFL
TGIGLDTTVMMRSIPLRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKKL
PTNQLQVTWEDHASGKEDTGTFDTVLWAIGRVPETRTLNLEKAGISTNPK
NQKIIVDAQEATSVPHIYAIGDVAEGRPELTPTAIKAGKLLAQRLFGKSS
TLMDYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHVEVYHAYYKPLEFT
VADRDASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASY
AQVMQTVGIHPTCSEEVVKLHISKRSGLEPTVTG
3D structure
PDB1zdl Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L82 C86 C91 K94 Y228 E232 G495 H497 E502 G521
Catalytic site (residue number reindexed from 1) L45 C49 C54 K57 Y191 E195 G458 H460 E465 G484
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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Biological Process

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Cellular Component
External links
PDB RCSB:1zdl, PDBe:1zdl, PDBj:1zdl
PDBsum1zdl
PubMed16217027
UniProtQ9JLT4|TRXR2_MOUSE Thioredoxin reductase 2, mitochondrial (Gene Name=Txnrd2)

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