Structure of PDB 2j3n Chain D

Receptor sequence
>2j3nD (length=491) Species: 9606 (Homo sapiens) [Search protein sequence]
KSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGT
CVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNH
IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFL
IATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGF
LAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQ
IEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVK
INEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLY
AGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWP
LEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKC
GLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCCG
3D structure
PDB2j3n The Structure of Human Thioredoxin Reductase 1 Provides Insights Into C-Terminal Rearrangements During Catalysis.
ChainD
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 G496 C497
Catalytic site (residue number reindexed from 1) L47 C51 C56 K59 Y192 E196 G462 H464 E469 G488 C489
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
View graph for
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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