Structure of PDB 7pm3 Chain D Binding Site BS01

Receptor Information
>7pm3 Chain D (length=371) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYV
GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLD
SGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTA
EREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER
FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ
MWITKQEYDEAGPSIVHRKCF
Ligand information
Ligand ID9UE
InChIInChI=1S/C36H45BrN4O6/c1-20-15-21(2)17-23(4)47-32(43)19-30(25-11-13-26(42)14-12-25)40-35(45)31(18-28-27-9-7-8-10-29(27)39-33(28)37)41(6)36(46)24(5)38-34(44)22(3)16-20/h7-15,21-24,30-31,39,42H,16-19H2,1-6H3,(H,38,44)(H,40,45)/b20-15+/t21-,22-,23-,24-,30+,31+/m0/s1
InChIKeyGQWYWHOHRVVHAP-DHKPLNAMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6CC1CC(OC(=O)CC(NC(=O)C(N(C(=O)C(NC(=O)C(CC(=C1)C)C)C)C)Cc2c3ccccc3[nH]c2Br)c4ccc(cc4)O)C
CACTVS 3.385C[CH]1C[CH](C)C=C(C)C[CH](C)C(=O)N[CH](C)C(=O)N(C)[CH](Cc2c(Br)[nH]c3ccccc23)C(=O)N[CH](CC(=O)O1)c4ccc(O)cc4
OpenEye OEToolkits 2.0.6C[C@@H]\1C[C@@H](OC(=O)C[C@@H](NC(=O)[C@H](N(C(=O)[C@@H](NC(=O)[C@H](C/C(=C1)/C)C)C)C)Cc2c3ccccc3[nH]c2Br)c4ccc(cc4)O)C
CACTVS 3.385C[C@H]1C[C@@H](C)\C=C(/C)C[C@H](C)C(=O)N[C@@H](C)C(=O)N(C)[C@H](Cc2c(Br)[nH]c3ccccc23)C(=O)N[C@H](CC(=O)O1)c4ccc(O)cc4
FormulaC36 H45 Br N4 O6
NameJasplakinolide
ChEMBLCHEMBL257166
DrugBank
ZINCZINC000028108899
PDB chain7pm3 Chain D Residue 401 [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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PDB7pm3 High-resolution structures of the actomyosin-V complex in three nucleotide states provide insights into the force generation mechanism.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		G197 Y198 S199 E205 Q246
Binding residue
(residue number reindexed from 1)		G193 Y194 S195 E201 Q242
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:7pm3, PDBe:7pm3, PDBj:7pm3
PDBsum7pm3
PubMed34812732
UniProtP68135|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

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