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BioLiP

Structure of PDB 6w17 Chain L

Receptor sequence
>6w17L (length=370) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYV
GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLD
SGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTA
EREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER
FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ
MWITKQEYDEAGPSIVHRKC
3D structure
PDB6w17 Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state.
ChainL
Resolution3.9 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 peptide L G197 Y198 S199 E205 Q246 G193 Y194 S195 E201 Q242
BS02 peptide L E72 H73 I75 R177 D179 E68 H69 I71 R173 D175
BS03 ADP L G13 K18 G156 D157 R210 E214 G302 M305 Y306 K336 G9 K14 G152 D153 R206 E210 G298 M301 Y302 K332
BS04 MG L Q137 G156 Q133 G152
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003785 actin monomer binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0005523 tropomyosin binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0019904 protein domain specific binding
GO:0031013 troponin I binding
GO:0031432 titin binding
GO:0032036 myosin heavy chain binding
GO:0042802 identical protein binding
GO:0048306 calcium-dependent protein binding
GO:0140660 cytoskeletal motor activator activity
Biological Process
GO:0010628 positive regulation of gene expression
GO:0030041 actin filament polymerization
GO:0030240 skeletal muscle thin filament assembly
GO:0048741 skeletal muscle fiber development
GO:0051017 actin filament bundle assembly
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:0031941 filamentous actin
GO:0032432 actin filament bundle
GO:0044297 cell body
GO:0098723 skeletal muscle myofibril

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Molecular Function

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Cellular Component
External links
PDB RCSB:6w17, PDBe:6w17, PDBj:6w17
PDBsum6w17
PubMed32839613
UniProtP68135|ACTS_RABIT Actin, alpha skeletal muscle (Gene Name=ACTA1)

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