Structure of PDB 8uxx Chain M

Receptor sequence
>8uxxM (length=370) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
TALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVG
DEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLL
TEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDS
GDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAE
REIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERF
RCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTM
YPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQM
WITKQEYDEAGPSIVHRKCF
3D structure
PDB8uxx High resolution cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by the Arp2/3 complex
ChainM
Resolution3.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ADP M G13 S14 G15 L16 K18 G156 D157 K213 E214 G301 G302 M305 Y306 G8 S9 G10 L11 K13 G151 D152 K208 E209 G296 G297 M300 Y301
BS02 BEF M S14 G156 D157 G158 S9 G151 D152 G153
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
PDBsum8uxx
PubMed38448439
UniProtP68139|ACTS_CHICK Actin, alpha skeletal muscle (Gene Name=ACTA1)

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