Structure of PDB 5nog Chain E

Receptor sequence
>5nogE (length=367) Species: 9823 (Sus scrofa) [Search protein sequence]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYV
GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLD
SGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTA
EREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER
FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ
MWISKQEYDEAGPSIVH
3D structure
PDB5nog Ca(2+)-induced movement of tropomyosin on native cardiac thin filaments revealed by cryoelectron microscopy.
ChainE
Resolution11.0 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 E S14 G15 L16 K18 G156 D157 G182 E214 G302 M305 Y306 K336 S10 G11 L12 K14 G152 D153 G178 E210 G298 M301 Y302 K332
BS02 MG E Q137 D154 Q133 D150
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:5nog, PDBe:5nog, PDBj:5nog
PDBsum5nog
PubMed28607071
UniProtP68137|ACTS_PIG Actin, alpha skeletal muscle (Gene Name=ACTA1)

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