Structure of PDB 2qc8 Chain E Binding Site BS04

Receptor Information
>2qc8 Chain E (length=355) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPE
WNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPA
ETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQG
PYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPC
EGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTK
AMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNI
NDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTC
LLNET
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 chain2qc8 Chain E Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2qc8 Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		W130 G132 E134 Q205 G207 P208 N255 S257 R324 Y336
Binding residue
(residue number reindexed from 1)		W121 G123 E125 Q196 G198 P199 N246 S248 R315 Y327
Annotation score5
Enzymatic activity
Enzyme Commision number 2.3.1.225: protein S-acyltransferase.
6.3.1.2: glutamine synthetase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0016874 ligase activity
GO:0019706 protein-cysteine S-palmitoyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0001525 angiogenesis
GO:0006538 glutamate catabolic process
GO:0006542 glutamine biosynthetic process
GO:0008283 cell population proliferation
GO:0009267 cellular response to starvation
GO:0009749 response to glucose
GO:0010594 regulation of endothelial cell migration
GO:0018345 protein palmitoylation
GO:0042254 ribosome biogenesis
GO:1903670 regulation of sprouting angiogenesis
GO:1904749 regulation of protein localization to nucleolus
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0044297 cell body
GO:0070062 extracellular exosome
GO:0097386 glial cell projection

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qc8, PDBe:2qc8, PDBj:2qc8
PDBsum2qc8
PubMed18005987
UniProtP15104|GLNA_HUMAN Glutamine synthetase (Gene Name=GLUL)

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