Structure of PDB 1get Chain B

Receptor sequence
>1getB (length=449) Species: 562 (Escherichia coli) [Search protein sequence]
TKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKK
VMWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYEN
VLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGV
EYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHA
PLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRS
ETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAV
GDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGT
VGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEK
IVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR
3D structure
PDB1get Anatomy of an engineered NAD-binding site.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L38 C42 C47 K50 Y177 E181 A437 H439 E444
Catalytic site (residue number reindexed from 1) L37 C41 C46 K49 Y176 E180 A436 H438 E443
Enzyme Commision number 1.8.1.7: glutathione-disulfide reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004362 glutathione-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
GO:0050661 NADP binding
GO:0071949 FAD binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0034599 cellular response to oxidative stress
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1get, PDBe:1get, PDBj:1get
PDBsum1get
PubMed7833810
UniProtP06715|GSHR_ECOLI Glutathione reductase (Gene Name=gor)

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