Structure of PDB 4pl7 Chain A Binding Site BS01

Receptor Information
>4pl7 Chain A (length=382) Species: 9606,644223 [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VAALVIDNGSGMCKAGYAGDDAPHTVFPSVVGSFVGDEAQSKRGILTLRY
PIEHGIVTNWDDMEKIWHHTFYNELRLAPEEHPVLLTEAPMNPKSNREKM
TQIMFETFNVPAFYVSIQAVLSLYASGRTTGIVLDSGDGVTHVVPIYAGF
SLPHAILRIDLAGRDLTDYLMKILSERGYTFSTSAEREIVRDIKEKLCYV
ALDFDQELQTSSQSSSIEKSYELPDGQVITIGNERFRAPEALFHPSVLGL
EASGIDQTTYNSIMKCDVDVRKELYSNIVMSGGTTMFPGIAERMQKELTA
LAPSSMKVKISAPPERKYSVWIGGSILASLGTFQQMWISKQEYDESDMAE
IEKFDKSKLKKTETQEKNPLPSKETIEQEKQA
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=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[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain4pl7 Chain A 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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PDB4pl7 Structural basis of thymosin-beta 4/profilin exchange leading to actin filament polymerization.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		G13 S14 G15 M16 K18 G156 D157 G158 G182 R210 K213 E214 G301 G302 M305 F306 K336
Binding residue
(residue number reindexed from 1)		G9 S10 G11 M12 K14 G137 D138 G139 G163 R191 K194 E195 G282 G283 M286 F287 K317
Annotation score5
Enzymatic activity
Enzyme Commision number ?
3.6.4.-
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003779 actin binding
GO:0003785 actin monomer binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0019899 enzyme binding
GO:0140311 protein sequestering activity
Biological Process
GO:0007015 actin filament organization
GO:0030334 regulation of cell migration
GO:0033209 tumor necrosis factor-mediated signaling pathway
GO:0042989 sequestering of actin monomers
GO:0043124 negative regulation of canonical NF-kappaB signal transduction
GO:0043536 positive regulation of blood vessel endothelial cell migration
GO:0050728 negative regulation of inflammatory response
GO:1905273 positive regulation of proton-transporting ATP synthase activity, rotational mechanism
GO:2001028 positive regulation of endothelial cell chemotaxis
GO:2001171 positive regulation of ATP biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0031093 platelet alpha granule lumen

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4pl7, PDBe:4pl7, PDBj:4pl7
PDBsum4pl7
PubMed25313062
UniProtP62328;
Q9P4D1|ACT_KOMPG Actin (Gene Name=ACT1)

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