Structure of PDB 6upw Chain D

Receptor sequence
>6upwD (length=370) Species: 9031 (Gallus gallus) [Search protein sequence]
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYV
GDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTL
LTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLD
SGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTA
EREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNER
FRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQ
MWITKQEYDEAGPSIVHRKC
3D structure
PDB6upw Molecular mechanism for direct actin force-sensing by alpha-catenin.
ChainD
Resolution2.9 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 D G13 S14 K18 D157 G182 K213 E214 G302 Y306 K336 G9 S10 K14 D153 G178 K209 E210 G298 Y302 K332
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:6upw, PDBe:6upw, PDBj:6upw
PDBsum6upw
PubMed32969337
UniProtP68139|ACTS_CHICK Actin, alpha skeletal muscle (Gene Name=ACTA1)

[Back to BioLiP]