Structure of PDB 2j3n Chain A

Receptor sequence
>2j3nA (length=486) Species: 9606 (Homo sapiens) [Search protein sequence]
SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTC
VNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHI
GSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLI
ATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFL
AGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQI
EAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKI
NEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYA
GSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPL
EWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCG
LTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQA
3D structure
PDB2j3n The Structure of Human Thioredoxin Reductase 1 Provides Insights Into C-Terminal Rearrangements During Catalysis.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L55 C59 C64 K67 Y200 E204 G470 H472 E477
Catalytic site (residue number reindexed from 1) L46 C50 C55 K58 Y191 E195 G461 H463 E468
Enzyme Commision number 1.11.1.2: NADPH peroxidase.
1.8.1.9: thioredoxin-disulfide reductase.
Interaction with ligand
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2j3n, PDBe:2j3n, PDBj:2j3n
PDBsum2j3n
PubMed17512005
UniProtQ16881|TRXR1_HUMAN Thioredoxin reductase 1, cytoplasmic (Gene Name=TXNRD1)

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