Structure of PDB 4b1u Chain B Binding Site BS01

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 IDLAB
InChIInChI=1S/C20H29NO5S/c1-13-5-3-4-6-14(2)9-18(22)25-16-10-15(8-7-13)26-20(24,11-16)17-12-27-19(23)21-17/h3,5,9,13,15-17,24H,4,6-8,10-12H2,1-2H3,(H,21,23)/b5-3-,14-9-/t13-,15-,16-,17+,20-/m1/s1
InChIKeyNSHPHXHGRHSMIK-JRIKCGFMSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C3OC2CC(OC(O)(C1NC(=O)SC1)C2)CCC(C=CCCC(=C3)C)C
CACTVS 3.341C[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\1
OpenEye OEToolkits 1.5.0C[C@H]\1CC[C@@H]2C[C@H](C[C@@](O2)([C@@H]3CSC(=O)N3)O)OC(=O)\C=C(/CC\C=C1)\C
OpenEye OEToolkits 1.5.0CC1CCC2CC(CC(O2)(C3CSC(=O)N3)O)OC(=O)C=C(CCC=C1)C
CACTVS 3.341C[CH]1CC[CH]2C[CH](C[C](O)(O2)[CH]3CSC(=O)N3)OC(=O)C=C(C)CCC=C1
FormulaC20 H29 N O5 S
NameLATRUNCULIN B
ChEMBLCHEMBL411879
DrugBankDB08080
ZINCZINC000005751767
PDB chain4b1u Chain B Residue 1376 [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)		G15 P32 Q59 Y69 D157 R183 T186 R206 E207 R210
Binding residue
(residue number reindexed from 1)		G11 P28 Q40 Y50 D138 R164 T167 R187 E188 R191
Annotation score1
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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