Structure of PDB 2d32 Chain A Binding Site BS03

Receptor Information
>2d32 Chain A (length=510) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGS
ALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMW
PLSMPSYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVH
YNFSLPMAFWQAKSGADAKEKISAGYFRVIRNYYRFGWVIPYLFGASPAI
SSSFLTSLPFEKTESGMYYLPYATSLRLSDLGYTNKSQSNLGITFNDLYE
YVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELYAPIRPKRV
TRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFMVWCA
LADAPEMSSSELACTRVNWNRVILEGRKPGLTLGIGCETAQFPLPQVGKD
LFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSARILRSMIDT
GIGGTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQEMEAADTE
PFAVWLEKHA
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2d32 Chain A Residue 1524 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2d32 Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		E27 E67
Binding residue
(residue number reindexed from 1)		E27 E67
Annotation score1
Enzymatic activity
Enzyme Commision number 6.3.2.2: glutamate--cysteine ligase.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2d32, PDBe:2d32, PDBj:2d32
PDBsum2d32
PubMed
UniProtP0A6W9|GSH1_ECOLI Glutamate--cysteine ligase (Gene Name=gshA)

[Back to BioLiP]