Structure of PDB 1h6v Chain D

Receptor sequence
>1h6vD (length=487) Species: 10116 (Rattus norvegicus) [Search protein sequence]
KSYDFDLIIIGGGSGGLAAAKEAAKFDKKVMVLDFVTPTPLGTNWGLGGT
CVNVGCIPKKLMHQAALLGQALKDSRNYGWKLEDTVKHDWEKMTESVQNH
IGSLNWGYRVALREKKVVYENAYGKFIGPHKIMATNNKGKEKVYSAERFL
IATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGF
LAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQ
IEAGTPGRLKVTAKSTNSEETIEDEFNTVLLAVGRDSCTRTIGLETVGVK
INEKTGKIPVTDEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLY
GGSTVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWP
LEWTVPSRDNNKCYAKVICNLKDNERVVGFHVLGPNAGEVTQGFAAALKC
GLTKQQLDSTIGIHPVCAEIFTTLSVTKRSGGDILQS
3D structure
PDB1h6v Three-Dimensional Structure of a Mammalian Thioredoxin Reductase: Implication for Mechanism and Evolution of a Selenocysteine Dependent Enzyme
ChainD
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) L55 C59 C64 K67 Y200 E204 G470 H472 E477
Catalytic site (residue number reindexed from 1) L47 C51 C56 K59 Y192 E196 G462 H464 E469
Enzyme Commision number 1.11.1.2: NADPH peroxidase.
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 D G21 S22 G23 L41 D42 F43 T58 C59 G63 C64 K67 A130 Y131 G132 T161 R293 D334 E341 L342 T343 G13 S14 G15 L33 D34 F35 T50 C51 G55 C56 K59 A122 Y123 G124 T153 R285 D326 E333 L334 T335
BS02 NDP D A198 S199 R221 S222 R226 V291 G292 A190 S191 R213 S214 R218 V283 G284
Gene Ontology
Molecular Function
GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
GO:0016174 NAD(P)H oxidase H2O2-forming activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0033797 selenate reductase activity
GO:0042802 identical protein binding
GO:0045340 mercury ion binding
GO:0050137 NADPH peroxidase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0001707 mesoderm formation
GO:0006979 response to oxidative stress
GO:0007369 gastrulation
GO:0008283 cell population proliferation
GO:0009410 response to xenobiotic stimulus
GO:0010269 response to selenium ion
GO:0016259 selenocysteine metabolic process
GO:0042537 benzene-containing compound metabolic process
GO:0042744 hydrogen peroxide catabolic process
GO:0043065 positive regulation of apoptotic process
GO:0045454 cell redox homeostasis
GO:0048678 response to axon injury
GO:0055093 response to hyperoxia
GO:0070276 halogen metabolic process
GO:0070995 NADPH oxidation
GO:0071280 cellular response to copper ion
GO:0071455 cellular response to hyperoxia
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0043025 neuronal cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h6v, PDBe:1h6v, PDBj:1h6v
PDBsum1h6v
PubMed11481439
UniProtO89049|TRXR1_RAT Thioredoxin reductase 1, cytoplasmic (Gene Name=Txnrd1)

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