Structure of PDB 8uxx Chain R Binding Site BS02
Receptor Information
>8uxx Chain R (length=370) Species:
9986
(Oryctolagus cuniculus) [
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TALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVG
DEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLL
TEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDS
GDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAE
REIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERF
RCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTM
YPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQM
WITKQEYDEAGPSIVHRKCF
Ligand information
Ligand ID
BEF
InChI
InChI=1S/Be.3FH/h;3*1H/q+2;;;/p-3
InChIKey
OGIAHMCCNXDTIE-UHFFFAOYSA-K
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
[Be-](F)(F)F
ACDLabs 10.04
CACTVS 3.341
F[Be-](F)F
Formula
Be F3
Name
BERYLLIUM TRIFLUORIDE ION
ChEMBL
DrugBank
ZINC
PDB chain
8uxx Chain R Residue 403 [
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Receptor-Ligand Complex Structure
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PDB
8uxx
High resolution cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by the Arp2/3 complex
Resolution
3.2 Å
Binding residue
(original residue number in PDB)
S14 Q137 G156 D157 G158
Binding residue
(residue number reindexed from 1)
S9 Q132 G151 D152 G153
Annotation score
1
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:0030240
skeletal muscle thin filament assembly
GO:0048741
skeletal muscle fiber development
Cellular Component
GO:0001725
stress fiber
GO:0005737
cytoplasm
GO:0005856
cytoskeleton
GO:0005865
striated muscle thin filament
GO:0005884
actin filament
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:8uxx
,
PDBe:8uxx
,
PDBj:8uxx
PDBsum
8uxx
PubMed
38448439
UniProt
P68139
|ACTS_CHICK Actin, alpha skeletal muscle (Gene Name=ACTA1)
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