Structure of PDB 1yvn Chain A Binding Site BS01

Receptor Information
>1yvn Chain A (length=372) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSY
VGDEAQSKRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPV
LLTEAPMNPKSNREKMTQIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVL
DSGDGNTHVVPIYAGFSLPHAILRIDLAGRDLTDYLMKILSERGYSFSTT
AEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSYELPDGQVITIGNE
RFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMSGGT
TMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQ
QMWISKQEYDESGPSIVHHKCF
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 chain1yvn Chain A Residue 378 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1yvn A change in actin conformation associated with filament instability after Pi release.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		G13 S14 G15 M16 K18 G156 D157 G158 N159 G182 K213 E214 G301 G302 M305 F306 K336
Binding residue
(residue number reindexed from 1)		G10 S11 G12 M13 K15 G153 D154 G155 N156 G179 K210 E211 G298 G299 M302 F303 K333
Annotation score5
Enzymatic activity
Enzyme Commision number 3.6.4.-
Gene Ontology
Molecular Function
GO:0005200 structural constituent of cytoskeleton
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
Biological Process
GO:0000011 vacuole inheritance
GO:0006281 DNA repair
GO:0006338 chromatin remodeling
GO:0006351 DNA-templated transcription
GO:0006355 regulation of DNA-templated transcription
GO:0006897 endocytosis
GO:0009306 protein secretion
GO:0030010 establishment of cell polarity
GO:0030476 ascospore wall assembly
GO:1902404 mitotic actomyosin contractile ring contraction
Cellular Component
GO:0000142 cellular bud neck contractile ring
GO:0000785 chromatin
GO:0000812 Swr1 complex
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005856 cytoskeleton
GO:0005884 actin filament
GO:0030479 actin cortical patch
GO:0031011 Ino80 complex
GO:0032432 actin filament bundle
GO:0035267 NuA4 histone acetyltransferase complex
GO:0043232 intracellular non-membrane-bounded organelle

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1yvn, PDBe:1yvn, PDBj:1yvn
PDBsum1yvn
PubMed
UniProtP60010|ACT_YEAST Actin (Gene Name=ACT1)

[Back to BioLiP]