Structure of PDB 1get Chain A

Receptor sequence
>1getA (length=448) Species: 562 (Escherichia coli) [Search protein sequence]
KHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKV
MWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENV
LGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVE
YGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAP
LRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDGSLTLELEDGRSE
TVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVG
DNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTV
GLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKI
VGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR
3D structure
PDB1get Anatomy of an engineered NAD-binding site.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) L36 C40 C45 K48 Y175 E179 A435 H437 E442
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

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

[Back to BioLiP]