Structure of PDB 5vdn Chain B

Receptor sequence
>5vdnB (length=449) Species: 187410 (Yersinia pestis KIM10+) [Search protein sequence]
TKHYDYLAIGGGSGGIASINRAAMYGKKCALIEAKQLGGTCVNVGCVPKK
VMWHAAQIAEAIHLYGPDYGFDTTVNHFDWKKLIANRTAYIDRIHQSYER
GLGNNKVDVIQGFARFVDAHTVEVNGETITADHILIATGGRPSHPDIPGA
EYGIDSDGFFELDEMPKRVAVVGAGYIAVEIAGVLNGLGTETHLFVRKHA
PLRTFDPLIVETLLEVMNTEGPKLHTESVPKAVIKNADGSLTLQLENGTE
VTVDHLIWAIGREPATDNLNLSVTGVKTNDKGYIEVDKFQNTNVKGIYAV
GDNTGVVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGT
IGLTEPQAREKFGDDQVKVYTSSFTAMYSAVTQHRQPCRMKLVCVGAEEK
IVGIHGIGFGMDEILQGFAVAMKMGATKKDFDNTVAIHPTAAEEFVTMR
3D structure
PDB5vdn 1.55 Angstrom Resolution Crystal Structure of Glutathione Reductase from Yersinia pestis in Complex with FAD.
ChainB
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L48 C52 C57 K60 Y187 E191 A447 H449 E454
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
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 B I20 G23 S24 G25 E44 A45 G50 T51 C52 G56 C57 K60 F124 A125 T149 G150 Y187 I188 R273 G312 D313 E319 L320 T321 I9 G12 S13 G14 E33 A34 G39 T40 C41 G45 C46 K49 F113 A114 T138 G139 Y176 I177 R262 G301 D302 E308 L309 T310
BS02 BDF B T51 G151 D168 T40 G140 D157
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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
Biological Process
GO:0006749 glutathione metabolic process
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:5vdn, PDBe:5vdn, PDBj:5vdn
PDBsum5vdn
PubMed
UniProtQ8CZL0

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