Structure of PDB 1sqk Chain A Binding Site BS03

Receptor Information
>1sqk Chain A (length=360) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGKDSYVGDEAQSK
RGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLN
PKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTH
NVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRD
IKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETL
FQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIAD
RMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQE
YDEAGPSIVH
Ligand information
Ligand IDLAR
InChIInChI=1S/C22H31NO5S/c1-15-7-5-3-4-6-8-16(2)11-20(24)27-18-12-17(10-9-15)28-22(26,13-18)19-14-29-21(25)23-19/h3-5,7,11,15,17-19,26H,6,8-10,12-14H2,1-2H3,(H,23,25)/b4-3+,7-5-,16-11-/t15-,17-,18-,19+,22-/m1/s1
InChIKeyDDVBPZROPPMBLW-IZGXTMSKSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.5C[C@H]/1CC[C@@H]2C[C@H](C[C@@](O2)([C@@H]3CSC(=O)N3)O)OC(=O)/C=C(\CC/C=C/C=C1)/C
CACTVS 3.385C[C@H]\1CC[C@@H]2C[C@H](C[C@@](O)(O2)[C@@H]3CSC(=O)N3)OC(=O)\C=C(C)/CC\C=C\C=C\1
ACDLabs 10.04O=C3OC2CC(OC(O)(C1NC(=O)SC1)C2)CCC(C=CC=CCCC(=C3)C)C
OpenEye OEToolkits 1.7.5CC1CCC2CC(CC(O2)(C3CSC(=O)N3)O)OC(=O)C=C(CCC=CC=C1)C
CACTVS 3.385C[CH]1CC[CH]2C[CH](C[C](O)(O2)[CH]3CSC(=O)N3)OC(=O)C=C(C)CCC=CC=C1
FormulaC22 H31 N O5 S
NameLATRUNCULIN A;
4-(17-HYDROXY-5,12-DIMETHYL-3-OXO-2,16-DIOXABICYCLO[13.3.1]NONADECA-4,8,10-TRIEN-17-YL)-2-THIAZOLIDINONE
ChEMBLCHEMBL404116
DrugBankDB02621
ZINCZINC000005766575
PDB chain1sqk 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

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PDB1sqk The beta-Thymosin/WH2 Domain; Structural Basis for the Switch from Inhibition to Promotion of Actin Assembly
Resolution2.5 Å
Binding residue
(original residue number in PDB)		G15 L16 P32 Q59 Y69 D157 G182 R183 T186 R206 E207 R210
Binding residue
(residue number reindexed from 1)		G11 L12 P28 Q48 Y58 D146 G171 R172 T175 R195 E196 R199
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.4.-
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003785 actin monomer binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0005523 tropomyosin binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0019904 protein domain specific binding
GO:0031013 troponin I binding
GO:0031432 titin binding
GO:0032036 myosin heavy chain binding
GO:0042802 identical protein binding
GO:0048306 calcium-dependent protein binding
GO:0140660 cytoskeletal motor activator activity
Biological Process
GO:0010628 positive regulation of gene expression
GO:0030041 actin filament polymerization
GO:0030240 skeletal muscle thin filament assembly
GO:0048741 skeletal muscle fiber development
GO:0051017 actin filament bundle assembly
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:0030027 lamellipodium
GO:0030175 filopodium
GO:0031941 filamentous actin
GO:0032432 actin filament bundle
GO:0044297 cell body
GO:0098723 skeletal muscle myofibril

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1sqk, PDBe:1sqk, PDBj:1sqk
PDBsum1sqk
PubMed15163409
UniProtP68135|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

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