Structure of PDB 2q1n Chain B Binding Site BS02

Receptor Information
>2q1n Chain B (length=344) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHLTLKYPIEHGIIT
NWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETF
NVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMR
LDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEM
ATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHET
TYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKI
KIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVH
Ligand information
Ligand IDANP
InChIInChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKeyPVKSNHVPLWYQGJ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)N[P](O)(O)=O)[C@@H](O)[C@H]3O
ACDLabs 12.01O=P(O)(O)NP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(NP(=O)(O)O)O)O)O)N
FormulaC10 H17 N6 O12 P3
NamePHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
ChEMBLCHEMBL1230989
DrugBank
ZINCZINC000008660410
PDB chain2q1n Chain B Residue 400 [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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PDB2q1n Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		G13 S14 G15 K18 G156 D157 G158 V159 G182 R210 K213 E214 G302 M305 Y306
Binding residue
(residue number reindexed from 1)		G10 S11 G12 K15 G129 D130 G131 V132 G155 R183 K186 E187 G275 M278 Y279
Annotation score3
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:2q1n, PDBe:2q1n, PDBj:2q1n
PDBsum2q1n
PubMed18391412
UniProtP68135|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

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