Structure of PDB 5nol Chain B

Receptor sequence
>5nolB (length=367) Species: 9823 (Sus scrofa) [Search protein sequence]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYV
GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLD
SGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTA
EREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER
FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ
MWISKQEYDEAGPSIVH
3D structure
PDB5nol Ca(2+)-induced movement of tropomyosin on native cardiac thin filaments revealed by cryoelectron microscopy.
ChainB
Resolution8.0 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 B G13 S14 L16 K18 G156 D157 K213 E214 G301 G302 T303 Y306 K336 G9 S10 L12 K14 G152 D153 K209 E210 G297 G298 T299 Y302 K332
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
Biological Process
GO:0010628 positive regulation of gene expression
GO:0030240 skeletal muscle thin filament assembly
GO:0048741 skeletal muscle fiber development
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:0044297 cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5nol, PDBe:5nol, PDBj:5nol
PDBsum5nol
PubMed28607071
UniProtP68137|ACTS_PIG Actin, alpha skeletal muscle (Gene Name=ACTA1)

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