Structure of PDB 2d33 Chain D

Receptor sequence
>2d33D (length=499) Species: 562 (Escherichia coli) [Search protein sequence]
MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGS
ALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMW
PLSMPSYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVH
YNFSLPMAFWQAKEKISAGYFRVIRNYYRFGWVIPYLFGASPAISSSFLS
LPFEKTESGMYYLPYATSLRLSDLGYTNSNLGITFNDLYEYVAGLKQAIK
TPSEEYAKIGIEKDGKRLQINSNVLQIENELYAPIRPKRVTRSGESPSDA
LLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFMVWCALADAPEMSSS
ELACTRVNWNRVILEGRKPGLTLGIGCETAQFPLPQVGKDLFRDLKRVAQ
TLDSINGGEAYQKVCDELVACFDNPDLTFSARILRSMIDTGIGGTGKAFA
EAYRNLLREEPLEILREEDFVAEREASERRQQEMEAADTEPFAVWLEKH
3D structure
PDB2d33 Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.
ChainD
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.2: glutamate--cysteine ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004357 glutamate-cysteine ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0046872 metal ion binding
Biological Process
GO:0006750 glutathione biosynthetic process
GO:0006972 hyperosmotic response
GO:0071243 cellular response to arsenic-containing substance
GO:0071288 cellular response to mercury ion
Cellular Component
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:2d33, PDBe:2d33, PDBj:2d33
PDBsum2d33
PubMed
UniProtP0A6W9|GSH1_ECOLI Glutamate--cysteine ligase (Gene Name=gshA)

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