Structure of PDB 8uxw Chain N

Receptor sequence
>8uxwN (length=370) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
TALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVG
DEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLL
TEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDS
GDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAE
REIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERF
RCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTM
YPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQM
WITKQEYDEAGPSIVHRKCF
3D structure
PDB8uxw High resolution cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by the Arp2/3 complex
ChainN
Resolution2.7 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 N G13 S14 G15 L16 K18 G156 D157 K213 E214 G302 T303 Y306 K336 G8 S9 G10 L11 K13 G151 D152 K208 E209 G297 T298 Y301 K331
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8uxw, PDBe:8uxw, PDBj:8uxw
PDBsum8uxw
PubMed38448439
UniProtP68139|ACTS_CHICK Actin, alpha skeletal muscle (Gene Name=ACTA1)

[Back to BioLiP]