Structure of PDB 1va6 Chain A Binding Site BS05

Receptor Information
>1va6 Chain A (length=507) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIPDVSQALAWLEKHPQALKGIQRGLERETLRVNADGTLATTGHPEALGS
ALTHKWITTDFAEALLEFITPVDGDIEHMLTFMRDLHRYTARNMGDERMW
PLSMPSYIAEGQDIELAQYGTSNTGRFKTLYREGLKNRYGALMQTISGVH
YNFSLPMAFWQAKSGDISGADAKEKISAGYFRVIRNYYRFGWVIPYLFGA
SPAISSSFLTSLPFEKTESGMYYLPYATSLRLSDLGYTNKSQSNLGITFN
DLYEYVAGLKQAIKTPSEEYAKIGIEKDGKRLQINSNVLQIENELYAPIR
PKRVTRSGESPSDALLRGGIEYIEVRSLDINPFSPIGVDEQQVRFLDLFM
VWCALADAPEMSSSELACTRVNWNRVILEGRKPGLTLGIGCETAQFPLPQ
VGKDLFRDLKRVAQTLDSINGGEAYQKVCDELVACFDNPDLTFSARILRS
MIDTTGKAFAEAYRNLLREEPLEILREEDFVAEREASERRQQEMEAADTE
PFAVWLE
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain1va6 Chain A Residue 521 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1va6 Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis
Resolution2.1 Å
Binding residue
(original residue number in PDB)		Q23 G25 E27 I69 T70 V72 N152 F153 S154 K306 Y326 E328
Binding residue
(residue number reindexed from 1)		Q23 G25 E27 I69 T70 V72 N152 F153 S154 K302 Y322 E324
Annotation score5
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1va6, PDBe:1va6, PDBj:1va6
PDBsum1va6
PubMed15477603
UniProtP0A6W9|GSH1_ECOLI Glutamate--cysteine ligase (Gene Name=gshA)

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