Structure of PDB 2hqm Chain A

Receptor sequence
>2hqmA (length=461) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
KHYDYLVIGGGSGGVASARRAASYGAKTLLVEAKALGGTCVNVGCVPKKV
MWYASDLATRVSHANEYGLYQNLPLDKEHLTFNWPEFKQKRDAYVHRLNG
IYQKNLEKEKVDVVFGWARFNKDGNVEVQKRDNTTEVYSANHILVATGGK
AIFPENIPGFELGTDSDGFFRLEEQPKKVVVVGAGYIGIELAGVFHGLGS
ETHLVIRGETVLRKFDECIQNTITDHYVKEGINVHKLSKIVKVEKNVTDK
LKIHMNDSKSIDDVDELIWTIGRKSHLGMGSENVGIKLNSHDQIIADEYQ
NTNVPNIYSLGDVVGKVELTPVAIAAGRKLSNRLFGPEKFRNDKLDYENV
PSVIFSHPEAGSIGISEKEAIEKYGKENIKVYNSKFTAMYYAMLSEKSPT
RYKIVCAGPNEKVVGLHIVGDSSAEILQGFGVAIKMGATKADFDNCVAIH
PTSAEELVTMR
3D structure
PDB2hqm Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L57 C61 C66 K69 Y207 E211 A470 H472 E477
Catalytic site (residue number reindexed from 1) L36 C40 C45 K48 Y186 E190 A448 H450 E455
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
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:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005777 peroxisome
GO:0005829 cytosol

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Molecular Function

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Cellular Component
External links
PDB RCSB:2hqm, PDBe:2hqm, PDBj:2hqm
PDBsum2hqm
PubMed17554778
UniProtP41921|GSHR_YEAST Glutathione reductase (Gene Name=GLR1)

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