Structure of PDB 4b1u Chain B Binding Site BS02

Receptor Information
>4b1u Chain B (length=349) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGSYVGDEAQSKRGILTLKY
PIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGY
ALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYV
ALDFENEMATEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHE
TTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMK
IKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF
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 chain4b1u Chain B Residue 1377 [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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PDB4b1u Structures of the Phactr1 RPEL domain and RPEL motif complexes with G-actin reveal the molecular basis for actin binding cooperativity.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G13 S14 G15 L16 K18 G156 D157 G158 G182 R210 K213 E214 G302 M305 Y306 K336
Binding residue
(residue number reindexed from 1)		G9 S10 G11 L12 K14 G137 D138 G139 G163 R191 K194 E195 G276 M279 Y280 K310
Annotation score5
Enzymatic activity
Enzyme Commision number 3.6.4.-
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
Biological Process
GO:0009612 response to mechanical stimulus
GO:0010628 positive regulation of gene expression
GO:0030240 skeletal muscle thin filament assembly
GO:0035865 cellular response to potassium ion
GO:0043503 skeletal muscle fiber adaptation
GO:0048545 response to steroid hormone
GO:0048741 skeletal muscle fiber development
GO:0090131 mesenchyme migration
Cellular Component
GO:0001725 stress fiber
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005865 striated muscle thin filament
GO:0005884 actin filament
GO:0015629 actin cytoskeleton
GO:0030017 sarcomere
GO:0030027 lamellipodium
GO:0030175 filopodium
GO:0032991 protein-containing complex
GO:0044297 cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4b1u, PDBe:4b1u, PDBj:4b1u
PDBsum4b1u
PubMed23041370
UniProtP68134|ACTS_MOUSE Actin, alpha skeletal muscle (Gene Name=Acta1)

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