Structure of PDB 4h0x Chain B Binding Site BS02

Receptor Information
>4h0x Chain B (length=358) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRKDSYVGDEAQSKRGILT
LKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANR
EKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIY
EGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKL
CYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSF
IGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKE
ITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAG
PSIVHRKC
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 chain4h0x Chain B Residue 403 [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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PDB4h0x Arginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complex
Resolution2.33 Å
Binding residue
(original residue number in PDB)		L16 P32 Q59 L67 Y69 D157 R183 T186 R206 E207 R210
Binding residue
(residue number reindexed from 1)		L12 P28 Q43 L51 Y53 D141 R167 T170 R190 E191 R194
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
View graph for
Cellular Component
External links
PDB RCSB:4h0x, PDBe:4h0x, PDBj:4h0x
PDBsum4h0x
PubMed23382240
UniProtP68135|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

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