Structure of PDB 2q0r Chain A Binding Site BS03

Receptor Information
>2q0r 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]
ALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQDSYVGDEAQSKRGIL
TLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKAN
REKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPI
YEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEK
LCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPS
FIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQK
EITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEA
GPSIVHRKCF
Ligand information
Ligand IDPXT
InChIInChI=1S/C47H68O14/c1-26-10-11-32-34(22-37(54-32)47(52)39(49)28(3)14-20-53-47)55-41(51)29(4)31-9-8-15-45(56-31)17-12-33(57-45)40(50)44(7)24-30(48)38(60-44)35-25-43(6)18-19-46(58-35,61-43)36-13-16-42(5,59-36)23-27(2)21-26/h10-11,21,27,29,31-38,40,49-50,52H,8-9,12-20,22-25H2,1-7H3/b11-10+,26-21+/t27-,29+,31-,32+,33-,34+,35+,36+,37-,38-,40-,42+,43-,44+,45+,46-,47+/m0/s1
InChIKeyUUHLZWPSPOPYFR-LTNDQFMQSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[C@@H]\1C[C@@]2(C)CC[C@@H](O2)[C@@]34CC[C@@](C)(C[C@@H](O3)[C@H]5O[C@](C)(CC5=O)[C@@H](O)[C@@H]6CC[C@@]7(CCC[C@H](O7)[C@@H](C)C(=O)O[C@@H]8C[C@H](O[C@@H]8/C=C/C(=C\1)/C)[C@@]9(O)OCCC(=C9O)C)O6)O4
OpenEye OEToolkits 1.5.0C[C@@H]/1C[C@]2(CC[C@@H](O2)[C@]34CC[C@](O3)(CC(O4)[C@@H]5C(=O)C[C@@](O5)([C@H]([C@@H]6CC[C@]7(O6)CCC[C@H](O7)[C@H](C(=O)O[C@@H]8C[C@H](O[C@@H]8\C=C\C(=C1)\C)[C@@]9(C(=C(CCO9)C)O)O)C)O)C)C)C
CACTVS 3.341C[CH]1C[C]2(C)CC[CH](O2)[C]34CC[C](C)(C[CH](O3)[CH]5O[C](C)(CC5=O)[CH](O)[CH]6CC[C]7(CCC[CH](O7)[CH](C)C(=O)O[CH]8C[CH](O[CH]8C=CC(=C1)C)[C]9(O)OCCC(=C9O)C)O6)O4
OpenEye OEToolkits 1.5.0CC1CC2(CCC(O2)C34CCC(O3)(CC(O4)C5C(=O)CC(O5)(C(C6CCC7(O6)CCCC(O7)C(C(=O)OC8CC(OC8C=CC(=C1)C)C9(C(=C(CCO9)C)O)O)C)O)C)C)C
ACDLabs 10.04O=C6OC2C(OC(C1(O)OCCC(=C1O)C)C2)C=CC(=CC(C)CC3(OC(CC3)C49OC(CC(O4)C5OC(C)(CC5=O)C(O)C8OC7(OC(C6C)CCC7)CC8)(C)CC9)C)C
FormulaC47 H68 O14
NamePECTENOTOXIN-2
ChEMBLCHEMBL1235520
DrugBank
ZINCZINC000263621103
PDB chain2q0r Chain A Residue 500 [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]
PDB2q0r A structural basis for regulation of actin polymerization by pectenotoxins.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		I75 P109 L110 N111 P112 I175 M176 R177
Binding residue
(residue number reindexed from 1)		I60 P94 L95 N96 P97 I160 M161 R162
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2q0r, PDBe:2q0r, PDBj:2q0r
PDBsum2q0r
PubMed17599353
UniProtP68135|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

[Back to BioLiP]