Structure of PDB 2d32 Chain A Binding Site BS07

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 IDANP
InChIInChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKeyPVKSNHVPLWYQGJ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
ACDLabs 12.01O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N
FormulaC10 H17 N6 O12 P3
NamePHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
ChEMBLCHEMBL1230989
DrugBank
ZINCZINC000008660410
PDB chain2d32 Chain A Residue 1521 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		Q23 G25 E27 I69 T70 V72 N152 S154 K306 Y326 E328
Binding residue
(residue number reindexed from 1)		Q23 G25 E27 I69 T70 V72 N152 S154 K298 Y318 E320
Annotation score3
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:2d32, PDBe:2d32, PDBj:2d32
PDBsum2d32
PubMed
UniProtP0A6W9|GSH1_ECOLI Glutamate--cysteine ligase (Gene Name=gshA)

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