Structure of PDB 3u9d Chain C Binding Site BS01

Receptor Information
>3u9d Chain C (length=357) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKA
NREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVP
IYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKE
KLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQP
SFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQ
KEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE
AGPSIVH
Ligand information
Receptor-Ligand Complex Structure
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PDB3u9d How a single residue in individual beta-thymosin/WH2 domains controls their functions in actin assembly.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		G23 D24 D25 Y143 A144 T148 E167 I345 L349 T351 M355
Binding residue
(residue number reindexed from 1)		G18 D19 D20 Y129 A130 T134 E153 I331 L335 T337 M341
Enzymatic activity
Enzyme Commision number 3.6.4.-
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
Biological Process
GO:0009612 response to mechanical stimulus
GO:0010628 positive regulation of gene expression
GO:0030240 skeletal muscle thin filament assembly
GO:0035865 cellular response to potassium ion
GO:0043503 skeletal muscle fiber adaptation
GO:0048545 response to steroid hormone
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:0015629 actin cytoskeleton
GO:0030017 sarcomere
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:3u9d, PDBe:3u9d, PDBj:3u9d
PDBsum3u9d
PubMed22193718
UniProtP68136|ACTS_RAT Actin, alpha skeletal muscle (Gene Name=Acta1)

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