Structure of PDB 5w1l Chain A

Receptor sequence
>5w1lA (length=584) Species: 6210 (Echinococcus granulosus) [Search protein sequence]
SAEQVEKLRNKINNAAVLVFAKSFCPYCKKVMERFNNLKIPFGYLDLDLK
KNGSDYQKMLQEITGRTTVPQVFFRGEFIGGCDDVMAIDDDTIVKKANEM
KYDYDMVIIGGGSGGLALAKESAKSGAKVALLDFVVPTPMGTTWGLGGTC
VNVGCIPKKLMHQAALLNHYMEDAKSFGWDVDKGPHDWVKMVEGIQDHIH
ALNFGYRSSMMNANVKYLNALGEIVDPHTIKTTNKQGIVKNITTNTIIVA
TGERPRYPPIPGAKEYGITSDDLFTLDHNPGKTLCVGASYVSLECAGFLS
SIGCDVTVMVRSIFLRGFDQQMAGLISDYIAKYGVKFVRPCVPTSVRCLE
EYDPESGKLAIYEVEGKHEDGTPFKDTFNTVLFAVGRDPCTTNIGLQNVD
VKTTNGRVVVDDEERTNVPNIYAIGDVSNAGYQLTPLAIQAGKNLARRLY
TADDCRTDYTNVPTTVFTPLEYGCIGLSEENAISKFGEDNIEVFHSYFQP
LEWTVPHRPDNTCYAKLIINKQDDNRVVGFHVFGPNAGEVTQGYAVAMHL
GARKEDFDRTIGIHPTCSETFTTLRVTKSSGASA
3D structure
PDB5w1l The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).
ChainA
Resolution2.88 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L152 C156 C161 K164 Y296 E300 G568 H570 E575
Catalytic site (residue number reindexed from 1) L146 C150 C155 K158 Y290 E294 G562 H564 E569
Enzyme Commision number 1.8.1.9: thioredoxin-disulfide reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004362 glutathione-disulfide reductase (NADPH) activity
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:0006749 glutathione metabolic process
GO:0034599 cellular response to oxidative stress
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5w1l, PDBe:5w1l, PDBj:5w1l
PDBsum5w1l
PubMed28463568
UniProtQ869D7

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